|
Name |
Accession |
Description |
Interval |
E-value |
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
6-272 |
0e+00 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 553.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLR 85
Cdd:PRK11172 1 MSIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 86 ESLEKLRTDRLDLVLIHWPAPGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEISTNQIELSPYLQ 165
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQIELSPYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 166 NRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLD 245
Cdd:PRK11172 161 NRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLD 240
|
250 260
....*....|....*....|....*..
gi 15599362 246 AEDMARIAGLERNGREVSPQGLAPAWD 272
Cdd:PRK11172 241 AEDMAAIAALDRNGRLVSPEGLAPEWD 267
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
8-255 |
7.38e-160 |
|
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: 443.72 E-value: 7.38e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRES 87
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAPGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEISTNQIELSPYLQNR 167
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPYLQNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 168 ALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAE 247
Cdd:cd19139 161 KLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDAD 240
|
....*...
gi 15599362 248 DMARIAGL 255
Cdd:cd19139 241 DMAAIAAL 248
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
8-260 |
7.24e-135 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 380.94 E-value: 7.24e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRES 87
Cdd:COG0656 5 IPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAAFEES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAPGNgveLGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAgEISTNQIELSPYLQNR 167
Cdd:COG0656 85 LERLGLDYLDLYLIHWPGPGP---YVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGV-KPAVNQVELHPYLQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 168 ALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAE 247
Cdd:COG0656 161 ELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDE 240
|
250
....*....|...
gi 15599362 248 DMARIAGLERNGR 260
Cdd:COG0656 241 DMAAIDALDRGER 253
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
6-255 |
2.51e-109 |
|
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: 316.12 E-value: 2.51e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLR 85
Cdd:cd19140 6 VRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLASVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 86 ESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAgEISTNQIELSPYLQ 165
Cdd:cd19140 86 ESLRKLRTDYVDLLLLHWPNK--DVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEA-PLFTNQVEYHPYLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 166 NRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAM-QLGYAVIPSSTRRENLASNLLARDLRL 244
Cdd:cd19140 163 QRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDIFDFTL 242
|
250
....*....|.
gi 15599362 245 DAEDMARIAGL 255
Cdd:cd19140 243 SDEEMARIAAL 253
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
8-252 |
1.03e-108 |
|
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: 314.21 E-value: 1.03e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRES 87
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGeISTNQIELSPYLQNR 167
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNP--TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP-IAVNQVEFHPFLYQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 168 ALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAE 247
Cdd:cd19073 158 ELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSE 237
|
....*
gi 15599362 248 DMARI 252
Cdd:cd19073 238 DVAKI 242
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
8-253 |
2.57e-103 |
|
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: 300.94 E-value: 2.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRES 87
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAPGNGVEL-GEYMA---ALAEAKSLGLTRRIGVSNFNIELTRQAIAAvgAGEI-STNQIELSP 162
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPGKEGGSkEARLEtwrALEELVDEGLVRSIGVSNFNVEHLEELLAA--ARIKpAVNQIELHP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 163 YLQNRALTAYLEEQGIAVTSYMTLA--YGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLAR 240
Cdd:cd19071 159 YLQQKELVEFCKEHGIVVQAYSPLGrgRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVF 238
|
250
....*....|...
gi 15599362 241 DLRLDAEDMARIA 253
Cdd:cd19071 239 DFELSEEDMAAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
6-256 |
1.12e-87 |
|
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: 261.54 E-value: 1.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLR 85
Cdd:cd19131 8 NTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDSTLRAFD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 86 ESLEKLRTDRLDLVLIHWPAPGNGVELgEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEiSTNQIELSPYLQ 165
Cdd:cd19131 88 ESLRKLGLDYVDLYLIHWPVPAQDKYV-ETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVP-VVNQIELHPRFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 166 NRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLD 245
Cdd:cd19131 166 QRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELD 245
|
250
....*....|.
gi 15599362 246 AEDMARIAGLE 256
Cdd:cd19131 246 ADDMQAIAGLD 256
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
6-257 |
4.81e-83 |
|
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: 249.49 E-value: 4.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLR 85
Cdd:cd19132 5 TQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEALRTIE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 86 ESLEKLRTDRLDLVLIHWPAPGNGVELgEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEiSTNQIELSPYLQ 165
Cdd:cd19132 85 ESLYRLGLDYVDLYLIHWPNPSRDLYV-EAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTP-AVNQIELHPYFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 166 NRALTAYLEEQGIAVTSYMTLAYG-KVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRL 244
Cdd:cd19132 163 QAEQRAYHREHGIVTQSWSPLGRGsGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFEL 242
|
250
....*....|...
gi 15599362 245 DAEDMARIAGLER 257
Cdd:cd19132 243 SDEDMAAIAALDR 255
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-262 |
1.15e-81 |
|
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: 247.71 E-value: 1.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAE----SGVPRSELFLTTKVWVDNYAREKLLAS 83
Cdd:cd19123 12 IPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEvfkeGKVKREDLWITSKLWNNSHAPEDVLPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWPA---PGNG-------------VELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIA- 146
Cdd:cd19123 92 LEKTLADLQLDYLDLYLMHWPValkKGVGfpesgedllslspIPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLAt 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 147 AVGAGEIstNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAYG------------KVLKDPTLAGIAARHRATVAQVALA 214
Cdd:cd19123 172 ARIKPAV--NQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdrpaamkaegepVLLEDPVINKIAEKHGASPAQVLIA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15599362 215 WAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGREV 262
Cdd:cd19123 250 WAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-260 |
9.47e-79 |
|
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: 238.83 E-value: 9.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRL-TGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRE 86
Cdd:cd19157 10 MPWLGLGVFKVeEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYDSTLKAFEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 87 SLEKLRTDRLDLVLIHWPAPGNGVELGEymaALAEAKSLGLTRRIGVSNFNIELTRQAIAavgAGEIS--TNQIELSPYL 164
Cdd:cd19157 90 SLERLGLDYLDLYLIHWPVKGKYKETWK---ALEKLYKDGRVRAIGVSNFQVHHLEDLLA---DAEIVpmVNQVEFHPRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 165 QNRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRL 244
Cdd:cd19157 164 TQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFEL 243
|
250
....*....|....*.
gi 15599362 245 DAEDMARIAGLERNGR 260
Cdd:cd19157 244 SQEDMDKIDALNENLR 259
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-255 |
9.51e-79 |
|
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: 238.63 E-value: 9.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 9 PSFGLGTFRLTG-QVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRES 87
Cdd:cd19133 10 PILGFGVFQIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEKAKKAFERS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPApGNgvelgEYMA--ALAEAKSLGLTRRIGVSNFNIELTRQAIAAVgagEI--STNQIELSPY 163
Cdd:cd19133 90 LKRLGLDYLDLYLIHQPF-GD-----VYGAwrAMEELYKEGKIRAIGVSNFYPDRLVDLILHN---EVkpAVNQIETHPF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 164 LQNRALTAYLEEQGIAVTSYMTLAYGK--VLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARD 241
Cdd:cd19133 161 NQQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFD 240
|
250
....*....|....
gi 15599362 242 LRLDAEDMARIAGL 255
Cdd:cd19133 241 FELSDEDMEAIAAL 254
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
8-255 |
2.26e-77 |
|
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: 235.22 E-value: 2.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQ-VVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAES----GVPRSELFLTTKVWVDNYAREKLLA 82
Cdd:cd19136 1 MPILGLGTFRLRGEeEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 83 SLRESLEKLRTDRLDLVLIHWPA--------PGNGVELGEYMAALAEAKSLGLTRRIGVSNFNI----ELTRQA--IAAV 148
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGvqglkpsdPRNAELRRESWRALEDLYKEGKLRAIGVSNYTVrhleELLKYCevPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 149 gageistNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAYG--KVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPS 226
Cdd:cd19136 161 -------NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGdlRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPK 233
|
250 260
....*....|....*....|....*....
gi 15599362 227 STRRENLASNLLARDLRLDAEDMARIAGL 255
Cdd:cd19136 234 STNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-260 |
1.60e-72 |
|
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: 224.08 E-value: 1.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTG-QVVVDSVRSALELGYRAIDTAQIYGNEADIGRA----IAESGVPRSELFLTTKVWVDNYAREKLLA 82
Cdd:cd19116 11 IPAIALGTWKLKDdEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNSYHEREQVEP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 83 SLRESLEKLRTDRLDLVLIHWP------------APGNGVELG--EYMAALAEAKSLGLTRRIGVSNFNIELTrQAIAAV 148
Cdd:cd19116 91 ALRESLKRLGLDYVDLYLIHWPvafkenndsesnGDGSLSDIDylETWRGMEDLVKLGLTRSIGVSNFNSEQI-NRLLSN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 149 GAGEISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAY---------GKVLKDPTLAGIAARHRATVAQVALAWAMQL 219
Cdd:cd19116 170 CNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRlvprgqtnpPPRLDDPTLVAIAKKYGKTTAQIVLRYLIDR 249
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599362 220 GYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGR 260
Cdd:cd19116 250 GVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQR 290
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-256 |
4.38e-72 |
|
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: 221.54 E-value: 4.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRL-TGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRE 86
Cdd:cd19126 9 MPWLGLGVFQTpDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARRTEDAFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 87 SLEKLRTDRLDLVLIHWPAPGNGVELGEYMAALAEAkslGLTRRIGVSNFNIELTRQaIAAVGAGEISTNQIELSPYLQN 166
Cdd:cd19126 89 SLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYAS---GKVKAIGVSNFQEHHLEE-LLAHADVVPAVNQVEFHPYLTQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 167 RALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDA 246
Cdd:cd19126 165 KELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSE 244
|
250
....*....|
gi 15599362 247 EDMARIAGLE 256
Cdd:cd19126 245 DDMTAIDALN 254
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-256 |
2.29e-71 |
|
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: 219.78 E-value: 2.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRES 87
Cdd:cd19130 10 IPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEPAAAFAES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAP--GNGVELGEYMAALAEAkslGLTRRIGVSNFNIELTRQAIAAVGAGEiSTNQIELSPYLQ 165
Cdd:cd19130 90 LAKLGLDQVDLYLVHWPTPaaGNYVHTWEAMIELRAA---GRTRSIGVSNFLPPHLERIVAATGVVP-AVNQIELHPAYQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 166 NRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLD 245
Cdd:cd19130 166 QRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLT 245
|
250
....*....|.
gi 15599362 246 AEDMARIAGLE 256
Cdd:cd19130 246 DTEIAAIDALD 256
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-260 |
1.82e-68 |
|
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: 212.76 E-value: 1.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLT-GQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRE 86
Cdd:cd19156 9 MPRLGLGVWRVQdGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYESTLAAFEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 87 SLEKLRTDRLDLVLIHWPAPGNGVELGEYMAALAEAKSLgltRRIGVSNFNIE-----LTRQAIAAVgageisTNQIELS 161
Cdd:cd19156 89 SLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKV---RAIGVSNFHEHhleelLKSCKVAPM------VNQIELH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 162 PYLQNRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARD 241
Cdd:cd19156 160 PLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFD 239
|
250
....*....|....*....
gi 15599362 242 LRLDAEDMARIAGLERNGR 260
Cdd:cd19156 240 FELTAEEIRQIDGLNTDHR 258
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-255 |
3.19e-68 |
|
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: 212.18 E-value: 3.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLtGQVVVDSVRSAL-ELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRE 86
Cdd:cd19135 13 MPILGLGTSHS-GGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYESTKQAFEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 87 SLEKLRTDRLDLVLIHWPAPGNGVE-----LGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAvgAGEIS-TNQIEL 160
Cdd:cd19135 92 SLKRLGVDYLDLYLLHWPDCPSSGKnvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLED--CSVVPhVNQVEF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 161 SPYLQNRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLAR 240
Cdd:cd19135 170 HPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVF 249
|
250
....*....|....*
gi 15599362 241 DLRLDAEDMARIAGL 255
Cdd:cd19135 250 DFSLSEEDMATLDSL 264
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
8-252 |
5.57e-68 |
|
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: 211.32 E-value: 5.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTG---------QVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIaeSGVPRSELFLTTKVWVDNY 75
Cdd:cd19072 4 VPVLGLGTWGIGGgmskdysddKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI--KGFDREDLFITTKVSPDHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 76 AREKLLASLRESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEIST 155
Cdd:cd19072 82 KYDDVIKAAKESLKRLGTDYIDLYLIHWPNP--SIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPIVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 156 NQIELSpyLQNR----ALTAYLEEQGIAVTSYMTLAYGKVLKD---PTLAGIAARHRATVAQVALAWAMQL-GYAVIPSS 227
Cdd:cd19072 160 NQVEYN--LFDReeesGLLPYCQKNGIAIIAYSPLEKGKLSNAkgsPLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKA 237
|
250 260
....*....|....*....|....*
gi 15599362 228 TRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19072 238 SNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
6-260 |
8.85e-68 |
|
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: 210.87 E-value: 8.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLR 85
Cdd:cd19134 9 NTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTASQAACR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 86 ESLEKLRTDRLDLVLIHWPAPGNGVELGEYmAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEiSTNQIELSPYLQ 165
Cdd:cd19134 89 ASLERLGLDYVDLYLIHWPAGREGKYVDSW-GGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTP-AVNQIELHPLLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 166 NRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLD 245
Cdd:cd19134 167 QAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELT 246
|
250
....*....|....*
gi 15599362 246 AEDMARIAGLERNGR 260
Cdd:cd19134 247 ADHMDALDGLDDGTR 261
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
7-257 |
1.35e-66 |
|
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: 208.24 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 7 PLPSFGLGT-----FRLTGQV-VVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNyarEKL 80
Cdd:cd19120 5 PAIAFGTGTawyksGDDDIQRdLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGI---KDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 81 LASLRESLEKLRTDRLDLVLIHWP--APGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIA------AVgage 152
Cdd:cd19120 82 REALRKSLAKLGVDYVDLYLIHSPffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDtakikpAV---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 153 istNQIELSPYLQNR--ALTAYLEEQGIAVTSYMTL------AYGKVlkDPTLAGIAARHRATVAQVALAWAMQLGYAVI 224
Cdd:cd19120 158 ---NQIEFHPYLYPQqpALLEYCREHGIVVSAYSPLspltrdAGGPL--DPVLEKIAEKYGVTPAQVLLRWALQKGIVVV 232
|
250 260 270
....*....|....*....|....*....|....*
gi 15599362 225 PSSTRRENLASNLLARDLRLDAEDMARI--AGLER 257
Cdd:cd19120 233 TTSSKEERMKEYLEAFDFELTEEEVEEIdkAGKQK 267
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-255 |
1.81e-66 |
|
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: 207.64 E-value: 1.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKLLASLRES 87
Cdd:cd19127 9 MPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKALRGFDAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAPGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEiSTNQIELSPYLQNR 167
Cdd:cd19127 89 LRRLGLDYVDLYLLHWPVPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVP-AVNQVELHPYFSQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 168 ALTAYLEEQGIAVTSYMTL------------AYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLAS 235
Cdd:cd19127 168 DLRAFHRRLGIVTQAWSPIggvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAE 247
|
250 260
....*....|....*....|
gi 15599362 236 NLLARDLRLDAEDMARIAGL 255
Cdd:cd19127 248 NIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-261 |
3.30e-66 |
|
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: 208.42 E-value: 3.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAE---SGV-PRSELFLTTKVWVDNYAREKLLAS 83
Cdd:cd19154 12 MPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHEHAPEDVEEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWPAP-----------GNG------VELGEYMAALAEAKSLGLTRRIGVSNFNIELTrQAIA 146
Cdd:cd19154 92 LRESLKKLQLEYVDLYLIHAPAAfkddegesgtmENGmsihdaVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQI-QRIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 147 AVGAGEISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAY---------------GKVLKDPTLAGIAARHRATVAQV 211
Cdd:cd19154 171 DNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstgvspaPNLLQDPIVKAIAEKHGKTPAQV 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15599362 212 ALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGRE 261
Cdd:cd19154 251 LLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-260 |
6.67e-64 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 201.45 E-value: 6.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKllASLRES 87
Cdd:PRK11565 15 MPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHKRPR--EALEES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAPgngvELGEYMAA---LAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEIsTNQIELSPYL 164
Cdd:PRK11565 93 LKKLQLDYVDLYLMHWPVP----AIDHYVEAwkgMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPV-INQIELHPLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 165 QNRALTAYLEEQGIAVTSYMTLAYG--KVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDL 242
Cdd:PRK11565 168 QQRQLHAWNATHKIQTESWSPLAQGgkGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDF 247
|
250
....*....|....*...
gi 15599362 243 RLDAEDMARIAGLERNGR 260
Cdd:PRK11565 248 RLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
4-256 |
1.17e-62 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 198.72 E-value: 1.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 4 TIHPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESG----VPRSELFLTTKVWVDNYAREK 79
Cdd:cd19125 7 TGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDHAPED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 80 LLASLRESLEKLRTDRLDLVLIHWPA--------PGNGVELG-------EYMAALAEAkslGLTRRIGVSNFNI----EL 140
Cdd:cd19125 87 VPPALEKTLKDLQLDYLDLYLIHWPVrlkkgahmPEPEEVLPpdipstwKAMEKLVDS---GKVRAIGVSNFSVkkleDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 141 TRQA--IAAVgageistNQIELSPYLQNRALTAYLEEQGIAVTSY-------MTLAYGKVLKDPTLAGIAARHRATVAQV 211
Cdd:cd19125 164 LAVArvPPAV-------NQVECHPGWQQDKLHEFCKSKGIHLSAYsplgspgTTWVKKNVLKDPIVTKVAEKLGKTPAQV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15599362 212 ALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLE 256
Cdd:cd19125 237 ALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIE 281
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-255 |
1.43e-59 |
|
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: 190.79 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESGVPRSELFLTTKVWVDNYAREKllASLRES 87
Cdd:cd19117 14 IPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHRRVE--EALDQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAPGN--GVELG--------------------EYMAALAeakSLGLTRRIGVSNFNIELTRQAI 145
Cdd:cd19117 92 LKKLGLDYVDLYLMHWPVPLDpdGNDFLfkkddgtkdhepdwdfiktwELMQKLP---ATGKVKAIGVSNFSIKNLEKLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 146 AAVGAGEI-STNQIELSPYLQNRALTAYLEEQGIAVTSYMTL--AYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYA 222
Cdd:cd19117 169 ASPSAKIVpAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLgsTNAPLLKEPVIIKIAKKHGKTPAQVIISWGLQRGYS 248
|
250 260 270
....*....|....*....|....*....|...
gi 15599362 223 VIPSSTRRENLASNLlaRDLRLDAEDMARIAGL 255
Cdd:cd19117 249 VLPKSVTPSRIESNF--KLFTLSDEEFKEIDEL 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
3-255 |
1.55e-58 |
|
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: 188.00 E-value: 1.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 3 STIHPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAES-----GVPRSELFLTTKVWVDNYAR 77
Cdd:cd19118 2 NTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSHRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 78 EKLLASLRESLEKLRTDRLDLVLIHWP---APGNG-------------------VELGEYMAALAEAKSLGLTRRIGVSN 135
Cdd:cd19118 82 EYVEPALDDTLKELGLDYLDLYLIHWPvafKPTGDlnpltavptnggevdldlsVSLVDTWKAMVELKKTGKVKSIGVSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 136 FNIELTRQAIAAvgAGEI-STNQIELSPYLQNRALTAYLEEQGIAVTSYMTL---AYGK--VLKDPTLAGIAARHRATVA 209
Cdd:cd19118 162 FSIDHLQAIIEE--TGVVpAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLplLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15599362 210 QVALAWAMQLGYAVIPSSTRRENLASNLlaRDLRLDAEDMARIAGL 255
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNF--EQVELSDDEFNAVTAL 283
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-252 |
1.57e-58 |
|
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: 187.46 E-value: 1.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRL-----TGQVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESgvpRSELFLTTKVWVDNYAREK 79
Cdd:cd19138 11 VPALGQGTWYMgedpaKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVLPSNASRQG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 80 LLASLRESLEKLRTDRLDLVLIHWPApgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEISTNQIE 159
Cdd:cd19138 88 TVRACERSLRRLGTDYLDLYLLHWRG---GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCAANQVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 160 LSpyLQNRA----LTAYLEEQGIAVTSYMTLAYG-----KVLKDPTLAGIAARHRATVAQVALAWAMQLGYAV-IPSSTR 229
Cdd:cd19138 165 YN--LGSRGieydLLPWCREHGVPVMAYSPLAQGgllrrGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGS 242
|
250 260
....*....|....*....|...
gi 15599362 230 RENLASNLLARDLRLDAEDMARI 252
Cdd:cd19138 243 PEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
6-264 |
2.42e-58 |
|
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: 188.08 E-value: 2.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAESG----VPRSELFLTTKVWvdNYAREKLL 81
Cdd:cd19112 9 HKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLW--NSDHGHVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 82 ASLRESLEKLRTDRLDLVLIHWPAPGNGVELGEYMAALAEAK---------------------SLGLTRRIGVSNFNIEL 140
Cdd:cd19112 87 EACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDGvldidvtislettwhameklvSAGLVRSIGISNYDIFL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 141 TRQAIA------AVgageistNQIELSPYLQNRALTAYLEEQGIAVTSYMTLA--------YGKV--LKDPTLAGIAARH 204
Cdd:cd19112 167 TRDCLAyskikpAV-------NQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaaanaewFGSVspLDDPVLKDLAKKY 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 205 RATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGREVSP 264
Cdd:cd19112 240 GKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQP 299
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
7-260 |
7.00e-58 |
|
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: 186.55 E-value: 7.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 7 PLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIA---ESG-VPRSELFLTTKVWVDNYAREKLLA 82
Cdd:cd19111 3 PMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDTEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 83 SLRESLEKLRTDRLDLVLIHWPApGNGVELGEYMAALAEAK------------SLGLTRRIGVSNFNIELTRQaIAAVGA 150
Cdd:cd19111 83 SLEKSLENLKLPYVDLYLIHHPC-GFVNKKDKGERELASSDvtsvwramealvSEGKVKSIGLSNFNPRQINK-ILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 151 GEISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTL-AYGKV-----------LKDPTLAGIAARHRATVAQVALAWAMQ 218
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgSPGRAnqslwpdqpdlLEDPTVLAIAKELDKTPAQVLLRFVLQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15599362 219 LGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGR 260
Cdd:cd19111 241 RGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-264 |
1.37e-57 |
|
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: 186.05 E-value: 1.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAES-----GVPRSELFLTTKVWVDNYAREKLLA 82
Cdd:cd19106 7 MPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHHPEDVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 83 SLRESLEKLRTDRLDLVLIHWPA---------PGNG--------VELGEYMAALAEAKSLGLTRRIGVSNFNielTRQA- 144
Cdd:cd19106 87 ALRKTLKDLQLDYLDLYLIHWPYafergdnpfPKNPdgtirydsTHYKETWKAMEKLVDKGLVKAIGLSNFN---SRQId 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 145 -IAAVGAGEISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTL-----AYGK-----VLKDPTLAGIAARHRATVAQVAL 213
Cdd:cd19106 164 dILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrPWAKpdepvLLEEPKVKALAKKYNKSPAQILL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15599362 214 AWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGREVSP 264
Cdd:cd19106 244 RWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVP 294
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
4-256 |
2.16e-56 |
|
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: 182.47 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 4 TIHPLPSFGLGT--FRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAE---SGV--PRSELFLTTKVWVDNYA 76
Cdd:cd19124 1 SGQTMPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGLvkSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 77 REKLLASLRESLEKLRTDRLDLVLIHWPA---PGNG---VELGEYM--------AALAEAKSLGLTRRIGVSNFNIELTR 142
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVslkPGKFsfpIEEEDFLpfdikgvwEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 143 Q--AIAAVGAgeiSTNQIELSPYLQNRALTAYLEEQGIAVTSYMTL-AYGK------VLKDPTLAGIAARHRATVAQVAL 213
Cdd:cd19124 161 EllSFATIPP---AVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgAPGTkwgsnaVMESDVLKEIAAAKGKTVAQVSL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15599362 214 AWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLE 256
Cdd:cd19124 238 RWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIP 280
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
12-255 |
2.35e-56 |
|
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: 182.51 E-value: 2.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTGQV-------VVDSVRSALELGYRAIDTAQIYG---NEADIGRAIAESGVPRSELFLTTKV------WVDNY 75
Cdd:pfam00248 2 GLGTWQLGGGWgpiskeeALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 76 AREKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAvGAGEIST 155
Cdd:pfam00248 82 SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIE--ETWDALEELKKEGKIRAIGVSNFDAEQIEKALTK-GKIPIVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 156 NQIELSPY--LQNRALTAYLEEQGIAVTSYMTLAYGKVLK---------------------------DPTLAGIAARHRA 206
Cdd:pfam00248 159 VQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnleaLEALEEIAKEHGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15599362 207 TVAQVALAWAMQ--LGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGL 255
Cdd:pfam00248 239 SPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
8-249 |
3.96e-55 |
|
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: 178.53 E-value: 3.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTG---------QVVVDSVRSALELGYRAIDTAQIYG---NEADIGRAIAEsgVPRSELFLTTKVWVDNY 75
Cdd:cd19137 4 IPALGLGTWGIGGfltpdysrdEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD--FPREDLFIVTKVWPTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 76 AREKLLASLRESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVgAGEIST 155
Cdd:cd19137 82 RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNP--NIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKS-QTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 156 NQIELSPY---LQNRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAV-IPSSTRRE 231
Cdd:cd19137 159 NQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVaIPKAGRVE 238
|
250
....*....|....*...
gi 15599362 232 NLASNLLARDLRLDAEDM 249
Cdd:cd19137 239 HLKENLKATEIKLSEEEM 256
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-260 |
1.96e-53 |
|
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: 175.41 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAE---SG-VPRSELFLTTKVWVDNYAREKLLAS 83
Cdd:cd19155 12 MPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLPPGGNRREKVEKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWPAPGNGVELGEY----------------------MAALAEAkslGLTRRIGVSNFNIE-L 140
Cdd:cd19155 92 LLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGkldptgehkqdyttdlldiwkaMEAQVDQ---GLTRSIGLSNFNREqM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 141 TRqaIAAVGAGEISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTL-----------------AYGKVLKDPTLAGIAAR 203
Cdd:cd19155 169 AR--ILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspgtgspsgSSPDLLQDPVVKAIAER 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599362 204 HRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGR 260
Cdd:cd19155 247 HGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-260 |
3.06e-53 |
|
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: 175.30 E-value: 3.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIG----RAIAESGVPRSELFLTTKVWVDNYAREKLLAS 83
Cdd:cd19115 13 MPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGqgvaRAIKEGIVKREDLFIVSKLWNTFHDGERVEPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWP-----------------APGNGVELG-----EYMAALAEAKSLGLTRRIGVSNFN---- 137
Cdd:cd19115 93 CRKQLADWGIDYFDLFLIHFPialkyvdpavryppgwfYDGKKVEFSnapiqETWTAMEKLVDKGLARSIGVSNFSaqll 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 138 IELTRQAiaavgagEI--STNQIELSPYLQNRALTAYLEEQGIAVTSYMTL--------------AYGKVLKDPTLAGIA 201
Cdd:cd19115 173 MDLLRYA-------RIrpATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFgpqsfleldlpgakDTPPLFEHDVIKSIA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599362 202 ARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGR 260
Cdd:cd19115 246 EKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
9-255 |
9.18e-53 |
|
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: 173.09 E-value: 9.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 9 PSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAE----SGVPRSELFLTTKVWVDNYAREKLLASL 84
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 85 RESLEKLRTDRLDLVLIHWP-----------APGNGVE-LGEY--------MAALAEAKslgLTRRIGVSNFNIELTRQA 144
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPlafdmdtdgdpRDDNQIQsLSKKpledtwraMEQCVDEK---LTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 145 IAAVGAGEIsTNQIELSPYLQNRALTAYLEEQGIAVTSYMTL----AYGK--VLKDPTLAGIAARHRATVAQVALAWAMQ 218
Cdd:cd19128 159 LNYCKIKPF-MNQIECHPYFQNDKLIKFCIENNIHVTAYRPLggsyGDGNltFLNDSELKALATKYNTTPPQVIIAWHLQ 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15599362 219 L---GYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGL 255
Cdd:cd19128 238 KwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
8-269 |
6.16e-50 |
|
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: 166.89 E-value: 6.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTG-------QVVVDSVRSALELGYRAIDTAQIYG---NEADIGRAIAesGVPRSELFLTTKV------- 70
Cdd:COG0667 13 VSRLGLGTMTFGGpwggvdeAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALK--GRPRDDVVIATKVgrrmgpg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 71 -WVDNYAREKLLASLRESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIA-AV 148
Cdd:COG0667 91 pNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDP--DTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAiAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 149 GAGEISTNQIELSpyLQNR----ALTAYLEEQGIAVTSYMTLAYG----KVLKDPT------------------------ 196
Cdd:COG0667 169 GLPPIVAVQNEYS--LLDRsaeeELLPAARELGVGVLAYSPLAGGlltgKYRRGATfpegdraatnfvqgylternlalv 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599362 197 --LAGIAARHRATVAQVALAWAMQLGY--AVIPSSTRRENLASNLLARDLRLDAEDMARIaglerngREVSPQGLAP 269
Cdd:COG0667 247 daLRAIAAEHGVTPAQLALAWLLAQPGvtSVIPGARSPEQLEENLAAADLELSAEDLAAL-------DAALAAVPAP 316
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-272 |
1.11e-49 |
|
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: 166.08 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIG----RAIAESGVPRSELFLTTKVWVDNYAREKLL 81
Cdd:cd19113 9 YKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGegvnRAIDEGLVKREELFLTSKLWNNFHDPKNVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 82 ASLRESLEKLRTDRLDLVLIHWP------------APG-----------NGVELGEYMAALAEAKSLGLTRRIGVSNFNI 138
Cdd:cd19113 89 TALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyPPGfycgdgdnfvyEDVPILDTWKALEKLVDAGKIKSIGVSNFPG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 139 ELTRQAIAAVGAGEISTnQIELSPYLQNRALTAYLEEQGIAVTSY--------MTLAYGKVLKDPTL------AGIAARH 204
Cdd:cd19113 169 ALILDLLRGATIKPAVL-QIEHHPYLQQPKLIEYAQKAGITITAYssfgpqsfVELNQGRALNTPTLfehdtiKSIAAKH 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599362 205 RATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGREVSPqglapaWD 272
Cdd:cd19113 248 NKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDP------WD 309
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
8-260 |
1.28e-49 |
|
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: 165.42 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGR----AIAESGVPRSELFLTTKVWVDNYAREKLLAS 83
Cdd:cd19114 4 MPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRgirkAIQEGLVKREDLFIVTKLWNNFHGKDHVREA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWPAPGNGVELGEYMAAL---AEAKSL--------------------GLTRRIGVSNFNIEL 140
Cdd:cd19114 84 FDRQLKDYGLDYIDLYLIHFPIPAAYVDPAENYPFLwkdKELKKFpleqspmqecwremeklvdaGLVRNIGIANFNVQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 141 TrqaIAAVGAGEISTN--QIELSPYLQNRALTAYLEEQGIAVTSYMTLA-------------YGKVLKDPTLAGIAARHR 205
Cdd:cd19114 164 I---LDLLTYAKIKPAvlQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGnavytkvtkhlkhFTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15599362 206 ATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGR 260
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
8-260 |
4.18e-49 |
|
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: 164.51 E-value: 4.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIA----ESGVPRSELFLTTKVWVDNYAREKLLAS 83
Cdd:cd19107 4 MPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQekikEQVVKREDLFIVSKLWCTFHEKGLVKGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWPA------------------PGNG--VELGEYMAALAEAkslGLTRRIGVSNFNIELTRQ 143
Cdd:cd19107 84 CQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnviPSDTtfLDTWEAMEELVDE---GLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 144 AIAAVGAG-EISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTLA-----YGK-----VLKDPTLAGIAARHRATVAQVA 212
Cdd:cd19107 161 ILNKPGLKyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpWAKpedpsLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15599362 213 LAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGR 260
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-249 |
1.78e-47 |
|
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: 159.23 E-value: 1.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIAES---GVPRSELFLTTKVWVDNYAREKLlaSL 84
Cdd:cd19121 12 IPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWSTYHRRVEL--CL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 85 RESLEKLRTDRLDLVLIHWPAPGNGVELGEYMAALAEAK--------------------SLGLTRRIGVSNFNIELTRQA 144
Cdd:cd19121 90 DRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDGSrdldwdwnhvdtwkqmekvlKTGKTKAIGVSNYSIPYLEEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 145 IAavgAGEI--STNQIELSPYLQNRALTAYLEEQGIAVTSYMTL--AYGKVLKDPTLAGIAARHRATVAQVALAWAMQLG 220
Cdd:cd19121 170 LK---HATVvpAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgsTGSPLISDEPVVEIAKKHNVGPGTVLISYQVARG 246
|
250 260
....*....|....*....|....*....
gi 15599362 221 YAVIPSSTRRENLASNLlaRDLRLDAEDM 249
Cdd:cd19121 247 AVVLPKSVTPDRIKSNL--EIIDLDDEDM 273
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
8-252 |
1.02e-46 |
|
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: 157.75 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTG---------QVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAEsgvPRSELFLTTKVWVDNY 75
Cdd:cd19085 1 VSRLGLGCWQFGGgywwgdqddEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 76 AREKLLASLRESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAavgAGEIST 155
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHWPSS--DVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALD---AGRIDS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 156 NQIelsPY-LQNRA----LTAYLEEQGIAVTSYMTLA-------YGKVLKDPT-------------------------LA 198
Cdd:cd19085 153 NQL---PYnLLWRAieyeILPFCREHGIGVLAYSPLAqglltgkFSSAEDFPPgdartrlfrhfepgaeeetfealekLK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599362 199 GIAARHRATVAQVALAWAMQLGY--AVIPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19085 230 EIADELGVTMAQLALAWVLQQPGvtSVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-260 |
4.04e-44 |
|
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: 151.23 E-value: 4.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRlTGQV----VVDSVRSALELGYRAIDTAQIYGNEADIGRAI----AESGVPRSELFLTTKVWVDNYAR 77
Cdd:cd19108 9 HFIPVLGFGTYA-PEEVpkskALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLWCTFHRP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 78 EKLLASLRESLEKLRTDRLDLVLIHWPAP-----------GNG------VELGEYMAALAEAKSLGLTRRIGVSNFNiel 140
Cdd:cd19108 88 ELVRPALEKSLKKLQLDYVDLYLIHFPVAlkpgeelfpkdENGklifdtVDLCATWEAMEKCKDAGLAKSIGVSNFN--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 141 TRQAiaavgagEI-----------STNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAYGK-----------VLKDPTLA 198
Cdd:cd19108 165 RRQL-------EMilnkpglkykpVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRdkewvdqnspvLLEDPVLC 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599362 199 GIAARHRATVAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGR 260
Cdd:cd19108 238 ALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
8-260 |
1.90e-42 |
|
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: 147.03 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAIA----ESGVPRSELFLTTKVWVDNYAREKLLAS 83
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIRekikEGVVRREDLFIVSKLWCTCHKKSLVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWP---APG--------NGVELGEYMAALAEAKSL------GLTRRIGVSNFNIELTRQAIA 146
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPmgfKPGepdlpldrSGMVIPSDTDFLDTWEAMedlvieGLVKNIGVSNFNHEQLERLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 147 AVGAG-EISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAYG----KVLKDPTLAGIAARHRATVAQVALAWAMQLGY 221
Cdd:cd19110 164 KPGLRvKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGScegvDLIDDPVIQRIAKKHGKSPAQILIRFQIQRNV 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 15599362 222 AVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGR 260
Cdd:cd19110 244 IVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLR 282
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
9-237 |
4.91e-42 |
|
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: 143.81 E-value: 4.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 9 PSFGLGTFRLTGQVVVDS----VRSALELGYRAIDTAQIYGN---EADIGRAIAESGVpRSELFLTTKV--------WVD 73
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEafalLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-RDDVVIATKGghppggdpSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 74 NYAREKLLASLRESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAV---GA 150
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDP--STPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAkahGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 151 GEISTNQIELS---PYLQNRALTAYLEEQGIAVTSYMTLAYGkvlkdptlagiaarhratVAQVALAWAMQLGY--AVIP 225
Cdd:cd06660 158 PGFAAVQPQYSlldRSPMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQPFvtVPIV 219
|
250
....*....|..
gi 15599362 226 SSTRRENLASNL 237
Cdd:cd06660 220 GARSPEQLEENL 231
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
8-262 |
2.60e-41 |
|
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: 144.17 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVD----SVRSALELGYRAIDTAQIYGNEADIGRA----IAESGVPRSELFLTTKVWVDNYAREK 79
Cdd:cd19109 4 IPIIGLGTYSEPKTTPKGacaeAVKVAIDTGYRHIDGAYIYQNEHEVGQAirekIAEGKVKREDIFYCGKLWNTCHPPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 80 LLASLRESLEKLRTDRLDLVLIHWP---APGNGV----ELGEYM----------AALAEAKSLGLTRRIGVSNFNielTR 142
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPmafKPGDEIyprdENGKWLyhktnlcatwEALEACKDAGLVKSIGVSNFN---RR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 143 QAIAAVGAGEIS----TNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAYGK-----------VLKDPTLAGIAARHRAT 207
Cdd:cd19109 161 QLELILNKPGLKhkpvSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRdpiwvnvssppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15599362 208 VAQVALAWAMQLGYAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLERNGREV 262
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYV 295
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-241 |
3.15e-41 |
|
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: 143.75 E-value: 3.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIGRAI----AESGVPRSELFLTTKVWVDNYAREKLLAS 83
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMqevfKAGKIRREDLFVTTKLWNTNHRPERVKPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWP---APG---------------NGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQaI 145
Cdd:cd19129 86 FEASLKRLQLDYLDLYLIHTPfafQPGdeqdprdangnviydDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLRE-I 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 146 AAVGAGEISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAYG---KVLKDPTLAGIAARHRATVAQVALAWAMQLGYA 222
Cdd:cd19129 165 FEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmepKLLEDPVITAIARRVNKTPAQVLLAWAIQRGTA 244
|
250 260
....*....|....*....|...
gi 15599362 223 VIPSSTR----RENLASNLLARD 241
Cdd:cd19129 245 LLTTSKTpsriRENFDISTLPED 267
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
23-252 |
1.63e-39 |
|
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: 138.90 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 23 VVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESGvPRSELFLTTKVWVDNY--AREKLLASLRESLEKLRTDRLD 97
Cdd:cd19093 28 LQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG-DRDEVVIATKFAPLPWrlTRRSVVKALKASLERLGLDSID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 98 LVLIHWPAPgNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAG--EISTNQIE---LSPYLQNRALTAY 172
Cdd:cd19093 107 LYQLHWPGP-WYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERgvPLASNQVEyslLYRDPEQNGLLPA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 173 LEEQGIAVTSYMTLAYG----------------------------KVLKDpTLAGIAARHRATVAQVALAWAMQLGYAVI 224
Cdd:cd19093 186 CDELGITLIAYSPLAQGlltgkyspenpppggrrrlfgrknlekvQPLLD-ALEEIAEKYGKTPAQVALNWLIAKGVVPI 264
|
250 260
....*....|....*....|....*...
gi 15599362 225 PSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19093 265 PGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-242 |
2.80e-39 |
|
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: 138.52 E-value: 2.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQV--VVDSVRSALELGYRAIDTAQIYGNEADIGRAIAE-----SGVPRSELFLTTKVWVDNYAREKL 80
Cdd:cd19122 9 IPAVGFGTFANEGAKgeTYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWNHLHEPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 81 LASLRESLEKLRTDRLDLVLIHWP--APGNGV------ELGEYMA-------------ALAEAKSLGLTRRIGVSNFNIE 139
Cdd:cd19122 89 KWSIDNSLKNLKLDYIDLFLVHWPiaAEKNDQrspklgPDGKYVIlkdltenpeptwrAMEEIYESGKAKAIGVSNWTIP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 140 LTRQ--AIAAVgagEISTNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAYG--------KVLKDPTLAGIAARHRATVA 209
Cdd:cd19122 169 GLKKllSFAKV---KPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQnqvpstgeRVSENPTLNEVAEKGGYSLA 245
|
250 260 270
....*....|....*....|....*....|...
gi 15599362 210 QVALAWAMQLGYAVIPSSTRRENLASNLLARDL 242
Cdd:cd19122 246 QVLIAWGLRRGYVVLPKSSTPSRIESNFKSIEL 278
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
8-252 |
7.41e-39 |
|
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: 137.27 E-value: 7.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTG--------QVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESgvpRSELFLTTKVWVD--- 73
Cdd:cd19084 4 VSRIGLGTWAIGGtwwgevddQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKCGLRwdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 74 ------NYAREKLLASLRESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAa 147
Cdd:cd19084 81 gkgvtkDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDP--NTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARK- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 148 vgAGEISTNQIELSPYLQN--RALTAYLEEQGIAVTSYMTLAYG----KVLKDPT------------------------- 196
Cdd:cd19084 158 --YGPIVSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQGlltgKYKKEPTfppddrrsrfpffrgenfeknleiv 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 197 --LAGIAARHRATVAQVALAWAMQ--LGYAVIPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19084 236 dkLKEIAEKYGKSLAQLAIAWTLAqpGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
8-245 |
7.28e-37 |
|
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: 131.19 E-value: 7.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQVV----------VDSVRSALELGYRAIDTAQIYG---NEADIGRAIAesgvPRSE-LFLTTKV--- 70
Cdd:cd19088 1 VSRLGYGAMRLTGPGIwgppadreeaIAVLRRALELGVNFIDTADSYGpdvNERLIAEALH----PYPDdVVIATKGglv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 71 ------WVDNYAREKLLASLRESLEKLRTDRLDLVLIHWPAPGngVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQA 144
Cdd:cd19088 77 rtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPK--VPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 145 IAAVgagEISTNQIELSP-YLQNRALTAYLEEQGIAVTSYMTLAYGKVLKD-PTLAGIAARHRATVAQVALAWAMQLG-- 220
Cdd:cd19088 155 RAIV---RIVSVQNRYNLaNRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPgGLLAEVAARLGATPAQVALAWLLARSpv 231
|
250 260
....*....|....*....|....*
gi 15599362 221 YAVIPSSTRRENLASNLLARDLRLD 245
Cdd:cd19088 232 MLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
6-249 |
9.53e-37 |
|
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: 131.85 E-value: 9.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTF--RLTGQVVVDSVRSALELGYRAIDTAQIYGNEADIG----RAIAESGVPRSELFLTTKVWVDNYarEK 79
Cdd:cd19119 10 ASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGeaikRAIDDGSIKREELFITTKVWPTFY--DE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 80 LLASLRESLEKLRTDRLDLVLIHWPAP----------------GNGVEL----GEYMAA---LAEAKSLGLTRRIGVSNF 136
Cdd:cd19119 88 VERSLDESLKALGLDYVDLLLVHWPVCfekdsddsgkpftpvnDDGKTRyaasGDHITTykqLEKIYLDGRAKAIGVSNY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 137 NIELTRQAIAAVgagEI--STNQIELSPYLQNRALTAYLEEQGIAVTSYMTLAYGK--VLKDPTLAGIAARHRATVAQVA 212
Cdd:cd19119 168 SIVYLERLIKEC---KVvpAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGapNLKNPLVKKIAEKYNVSTGDIL 244
|
250 260 270
....*....|....*....|....*....|....*..
gi 15599362 213 LAWAMQLGYAVIPSSTRRENLASNLlaRDLRLDAEDM 249
Cdd:cd19119 245 ISYHVRQGVIVLPKSLKPVRIVSNG--KIVSLTKEDL 279
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-255 |
1.83e-36 |
|
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: 131.26 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 23 VVDSVRSALELGYRAIDTAQIYG---NEADIGRAIAESgvpRSELFLTTK---VWVDN------YAREKLLASLRESLEK 90
Cdd:cd19102 28 SIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKGL---RDRPIVATKcglLWDEEgrirrsLKPASIRAECEASLRR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 91 LRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIELTRQaIAAVGAgeISTNQIELSpyLQNRALT 170
Cdd:cd19102 105 LGVDVIDLYQIHWPDPDEPIE--EAWGALAELKEEGKVRAIGVSNFSVDQMKR-CQAIHP--IASLQPPYS--LLRRGIE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 171 A----YLEEQGIAVTSYMTLAYG---------KVLKDP------------------------TLAGIAARHRATVAQVAL 213
Cdd:cd19102 178 AeilpFCAEHGIGVIVYSPMQSGlltgkmtpeRVASLPaddwrrrspffqepnlarnlalvdALRPIAERHGRTVAQLAI 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15599362 214 AWAMQLG--YAVIPSSTRRENLASNLLARDLRLDAEDMARIAGL 255
Cdd:cd19102 258 AWVLRRPevTSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
13-248 |
7.50e-35 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 126.80 E-value: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 13 LGTFRLTG-----QVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESGVPRSELFLTTK---VWVD-------- 73
Cdd:COG4989 18 LGCMRLGEwdlspAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLSPSLREKIELQTKcgiRLPSeardnrvk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 74 --NYAREKLLASLRESLEKLRTDRLDLVLIHWPAPGngVELGEYMAALAEAKSLGLTRRIGVSNFN---IELTRQAIAAv 148
Cdd:COG4989 98 hyDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPL--MDPEEVAEAFDELKASGKVRHFGVSNFTpsqFELLQSALDQ- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 149 gagEISTNQIELSPyLQNRALT----AYLEEQGIAVTSYMTLAYGKVLKDPT---------LAGIAARHRATVAQVALAW 215
Cdd:COG4989 175 ---PLVTNQIELSL-LHTDAFDdgtlDYCQLNGITPMAWSPLAGGRLFGGFDeqfprlraaLDELAEKYGVSPEAIALAW 250
|
250 260 270
....*....|....*....|....*....|....*
gi 15599362 216 AMQLGYAVIP--SSTRRENLASNLLARDLRLDAED 248
Cdd:COG4989 251 LLRHPAGIQPviGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
7-252 |
1.05e-31 |
|
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: 118.43 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 7 PLPSFGLGTFRLTG-----QVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESGVPRSELFLTTKV-------- 70
Cdd:cd19092 5 EVSRLVLGCMRLADwgesaEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKCgirlgddp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 71 ---WVDNY--AREKLLASLRESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFN---IELTR 142
Cdd:cd19092 85 rpgRIKHYdtSKEHILASVEGSLKRLGTDYLDLLLLHRPDP--LMDPEEVAEAFDELVKSGKVRYFGVSNFTpsqIELLQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 143 QAIaavgAGEISTNQIELSPY----LQNRALtAYLEEQGIAVTSYMTLAYGKVLKDPT---------LAGIAARHRATVA 209
Cdd:cd19092 163 SYL----DQPLVTNQIELSLLhteaIDDGTL-DYCQLLDITPMAWSPLGGGRLFGGFDerfqrlraaLEELAEEYGVTIE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15599362 210 QVALAWAMQLGYAVIP--SSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19092 238 AIALAWLLRHPARIQPilGTTNPERIRSAVKALDIELTREEWYEI 282
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
12-239 |
1.19e-30 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 114.64 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTGQVVVDS-------VRSALELGYRAIDTAQIYGN-EADIGRAIAesGVPRSELFLTTKVW--------VDNY 75
Cdd:cd19095 4 GLGTSGIGRVWGVPSeaeaarlLNTALDLGINLIDTAPAYGRsEERLGRALA--GLRRDDLFIATKVGthgeggrdRKDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 76 AREKLLASLRESLEKLRTDRLDLVLIHwpAPGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELtrqaIAAVGAGEIST 155
Cdd:cd19095 82 SPAAIRASIERSLRRLGTDYIDLLQLH--GPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGEEL----EAAIASGVFDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 156 NQIELSPYLQ-NRALTAYLEEQGIAVTSYMTLAYG----KVLKDPTLAGIAARHRA-------TVAQVALAWAMQ--LGY 221
Cdd:cd19095 156 VQLPYNVLDReEEELLPLAAEAGLGVIVNRPLANGrlrrRVRRRPLYADYARRPEFaaeiggaTWAQAALRFVLShpGVS 235
|
250
....*....|....*...
gi 15599362 222 AVIPSSTRRENLASNLLA 239
Cdd:cd19095 236 SAIVGTTNPEHLEENLAA 253
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
8-257 |
6.08e-30 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 115.30 E-value: 6.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRL---TGQVVVDSVRSALELGYRAIDTAQIYGN-EADIGRAIAEsgvPRSELFLTTK--VWVDNyaREKLL 81
Cdd:COG1453 13 VSVLGFGGMRLprkDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKlpPWVRD--PEDMR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 82 ASLRESLEKLRTDRLDLVLIH-------WPAPGNGvelGEYMAALAEAKSLGLTRRIGVSNFN-IELtrqAIAAVGAGEI 153
Cdd:COG1453 88 KDLEESLKRLQTDYIDLYLIHglnteedLEKVLKP---GGALEALEKAKAEGKIRHIGFSTHGsLEV---IKEAIDTGDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 154 STNQIELSPYLQN----RALTAYLEEQGIAVTSyM-TLAYGKVLKDPTLAGIAARHRATVAQVALAWAMQLGYAVIPSS- 227
Cdd:COG1453 162 DFVQLQYNYLDQDnqagEEALEAAAEKGIGVII-MkPLKGGRLANPPEKLVELLCPPLSPAEWALRFLLSHPEVTTVLSg 240
|
250 260 270
....*....|....*....|....*....|...
gi 15599362 228 -TRRENLASNL--LARDLRLDAEDMARIAGLER 257
Cdd:COG1453 241 mSTPEQLDENLktADNLEPLTEEELAILERLAE 273
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
12-252 |
2.45e-29 |
|
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: 112.75 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTG---------QVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESgvpRSELFLTTK---VW----- 71
Cdd:cd19149 15 GLGTWAIGGgpwwggsddNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcglRWdregg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 72 -----------VDNYAREKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIEl 140
Cdd:cd19149 92 sfffvrdgvtvYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIE--ETMEALEELKRQGKIRAIGASNVSVE- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 141 trQAIAAVGAGEISTNQIELSpyLQNRA----LTAYLEEQGIAVTSYMTLAYG----KVLKDPTLAG------------- 199
Cdd:cd19149 169 --QIKEYVKAGQLDIIQEKYS--MLDRGiekeLLPYCKKNNIAFQAYSPLEQGlltgKITPDREFDAgdarsgipwfspe 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599362 200 --------------IAARHRATVAQVALAWAM-QLGY-AVIPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19149 245 nrekvlallekwkpLCEKYGCTLAQLVIAWTLaQPGItSALCGARKPEQAEENAKAGDIRLSAEDIATM 313
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
24-252 |
2.66e-28 |
|
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: 109.82 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 24 VDSVRSALELGYRAIDTAQIYG---NEADIGRAIAESGvpRSELFLTTK---------VWVDNyAREKLLASLRESLEKL 91
Cdd:cd19083 36 KDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYN--RNEVVIATKgahkfggdgSVLNN-SPEFLRSAVEKSLKRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 92 RTDRLDLVLIHWPAPGngVELGEYMAALAEAKSLGLTRRIGVSNFNIEltrQAIAAVGAGEISTNQIELSpYLQNRALTA 171
Cdd:cd19083 113 NTDYIDLYYIHFPDGE--TPKAEAVGALQELKDEGKIRAIGVSNFSLE---QLKEANKDGYVDVLQGEYN-LLQREAEED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 172 ---YLEEQGIAVTSYMTLAY----GKVLKDPT---------------------------LAGIAARHRATVAQVALAWAM 217
Cdd:cd19083 187 ilpYCVENNISFIPYFPLASgllaGKYTKDTKfpdndlrndkplfkgerfsenldkvdkLKSIADEKGVTVAHLALAWYL 266
|
250 260 270
....*....|....*....|....*....|....*..
gi 15599362 218 Q--LGYAVIPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19083 267 TrpAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFI 303
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
12-239 |
1.21e-27 |
|
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: 106.41 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTGQV--------VVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAEsgvPRSELFLTTKV---------W 71
Cdd:cd19086 7 GFGTWGLGGDWwgdvddaeAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFgnrfdggpeR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 72 VDNYAREKLLASLRESLEKLRTDRLDLVLIHWPaPGNGVELGEYMAALAEAKSLGLTRRIGVSnfnIELTRQAIAAVGAG 151
Cdd:cd19086 84 PQDFSPEYIREAVEASLKRLGTDYIDLYQLHNP-PDEVLDNDELFEALEKLKQEGKIRAYGVS---VGDPEEALAALRRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 152 EISTNQIELSPYLQN--RALTAYLEEQGIAVTSYMTLAYGkvlkdpTLAGiaarhraTVAQVALAWAmqLGY----AVIP 225
Cdd:cd19086 160 GIDVVQVIYNLLDQRpeEELFPLAEEHGVGVIARVPLASG------LLTG-------KLAQAALRFI--LSHpavsTVIP 224
|
250
....*....|....
gi 15599362 226 SSTRRENLASNLLA 239
Cdd:cd19086 225 GARSPEQVEENAAA 238
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
30-252 |
3.22e-27 |
|
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: 106.92 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 30 ALELGYRAIDTAQIYG---NEADIGRAIAEsgvPRSELFLTTK---VWVD-------NYAREKLLASLRESLEKLRTDRL 96
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVIATKfgiVRDPgsgfrgvDGRPEYVRAACEASLKRLGTDVI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 97 DLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIELTRQA-----IAAVgageistnQIELSPYLQN--RAL 169
Cdd:cd19076 118 DLYYQHRVDPNVPIE--ETVGAMAELVEEGKVRYIGLSEASADTIRRAhavhpITAV--------QSEYSLWTRDieDEV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 170 TAYLEEQGIAVTSYMTLAYG----------KVLKD------PTLAG---------------IAARHRATVAQVALAWAMQ 218
Cdd:cd19076 188 LPTCRELGIGFVAYSPLGRGfltgaikspeDLPEDdfrrnnPRFQGenfdknlklvekleaIAAEKGCTPAQLALAWVLA 267
|
250 260 270
....*....|....*....|....*....|....*.
gi 15599362 219 LGYAV--IPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19076 268 QGDDIvpIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-252 |
5.13e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 106.14 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 20 GQVVVDSVRSALELGYRAIDTAQIYGN-EADIGRAIAESG---------------VPRSELFLTTKVWVDnyarekllAS 83
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRrerdaaddvqihtkwVPDPGELTMTRAYVE--------AA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHW--PAPGNGVELGEYMAALAEAkslGLTRRIGVSNFNIELTRQAIAAVgaGEISTNQIELS 161
Cdd:cd19101 94 IDRSLKRLGVDRLDLVQFHWwdYSDPGYLDAAKHLAELQEE---GKIRHLGLTNFDTERLREILDAG--VPIVSNQVQYS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 162 pYLQNRA---LTAYLEEQGIAVTSYMTLAYG---------------------------------------KVLKdpTLAG 199
Cdd:cd19101 169 -LLDRRPengMAALCEDHGIKLLAYGTLAGGllsekylgvpeptgpaletrslqkyklmidewggwdlfqELLR--TLKA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599362 200 IAARHRATVAQVALAWAMQ---LGyAVIPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19101 246 IADKHGVSIANVAVRWVLDqpgVA-GVIVGARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-237 |
4.52e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 102.66 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRlTGQVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAesGVPRSELFLTTKVWV--DNYAREKLLASLRE 86
Cdd:cd19105 17 GFGGGG-LPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPrlDKKDKAELLKSVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 87 SLEKLRTDRLDLVLIHWPAPGNGVEL-GEYMAALAEAKSLGLTRRIGVS-NFNIEltRQAIAAVGAGEISTNQI----EL 160
Cdd:cd19105 94 SLKRLQTDYIDIYQLHGVDTPEERLLnEELLEALEKLKKEGKVRFIGFStHDNMA--EVLQAAIESGWFDVIMVaynfLN 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599362 161 SPYLQNRALTAyLEEQGIAVTSYMTLAYGKVLKDPTLAGIAArhRATVAQVALAWAMQLGY--AVIPSSTRRENLASNL 237
Cdd:cd19105 172 QPAELEEALAA-AAEKGIGVVAMKTLAGGYLQPALLSVLKAK--GFSLPQAALKWVLSNPRvdTVVPGMRNFAELEENL 247
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
32-252 |
7.69e-26 |
|
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: 103.06 E-value: 7.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 32 ELGYRAIDTAQIYGN----------EADIGRAIAESGvPRSELFLTTKV----WVDNY--AREKLLASLRESLEKLRTDR 95
Cdd:cd19081 37 DAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSRG-KRDRVVIATKVgfpmGPNGPglSRKHIRRAVEASLRRLQTDY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 96 LDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIaavgagEISTnQIELSPY--------LQNR 167
Cdd:cd19081 116 IDLYQAHWDDP--ATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEAL------ELSR-QHGLPRYvslqpeynLVDR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 168 ALTAY-----LEEQGIAVTSYMTLA----YGKVLKDPTLAG-------------------------IAARHRATVAQVAL 213
Cdd:cd19081 187 ESFEGellplCREEGIGVIPYSPLAggflTGKYRSEADLPGstrrgeaakrylnerglrildaldeVAAEHGATPAQVAL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599362 214 AWAMQLGY--AVIPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19081 267 AWLLARPGvtAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
12-145 |
4.89e-25 |
|
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: 100.32 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTG-------QVVVDSVRSALELGYRAIDTAQIYGN-EADIGRAIAEsgVPRSELFLTTKV-----WVDNYARE 78
Cdd:cd19090 4 GLGTAGLGGvfggvddDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE--LPREPLVLSTKVgrlpeDTADYSAD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 79 KLLASLRESLEKLRTDRLDLVLIH---WPAPGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAI 145
Cdd:cd19090 82 RVRRSVEESLERLGRDRIDLLMIHdpeRVPWVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAI 151
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
27-252 |
8.11e-25 |
|
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: 100.74 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 27 VRSALELGYRAIDTAQIYGN---EADIGRAIAESGvPRSELFLTTKVW--VDNYA------REKLLASLRESLEKLRTDR 95
Cdd:cd19079 41 IKRALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVVIATKVYfpMGDGPngrglsRKHIMAEVDASLKRLGTDY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 96 LDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFnieLTRQAIAAVGAGEIStnqiELSPY--LQN------- 166
Cdd:cd19079 120 IDLYQIHRWDYETPIE--ETLEALHDVVKSGKVRYIGASSM---YAWQFAKALHLAEKN----GWTKFvsMQNhynllyr 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 167 ---RALTAYLEEQGIAVTSYMTLAYG----------KVLKDPTLAG--------------------IAARHRATVAQVAL 213
Cdd:cd19079 191 eeeREMIPLCEEEGIGVIPWSPLARGrlarpwgdttERRRSTTDTAklkydyfteadkeivdrveeVAKERGVSMAQVAL 270
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599362 214 AWAMQLGYAVIP--SSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19079 271 AWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-237 |
8.49e-25 |
|
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: 98.71 E-value: 8.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGT---FRLTGQVVVDSVRSALELGYRAIDTAQIYGN-EADIGRAIAEsgvPRSELFLTTKVWVDNYarEKLLASLRES 87
Cdd:cd19100 15 GFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGARDY--EGAKRDLERS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPAPGNGVEL----GEYMAALAEAKSLGLTRRIGVSNFNIELtrqAIAAVGAGEISTNQIELSP- 162
Cdd:cd19100 90 LKRLGTDYIDLYQLHAVDTEEDLDQvfgpGGALEALLEAKEEGKIRFIGISGHSPEV---LLRALETGEFDVVLFPINPa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 163 YLQNR----ALTAYLEEQGIAVTSYMTLAYGKVLKDPTLagiaarhraTVAQvALAWAMQLGY--AVIPSSTRRENLASN 236
Cdd:cd19100 167 GDHIDsfreELLPLAREKGVGVIAMKVLAGGRLLSGDPL---------DPEQ-ALRYALSLPPvdVVIVGMDSPEELDEN 236
|
.
gi 15599362 237 L 237
Cdd:cd19100 237 L 237
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
31-241 |
1.10e-22 |
|
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: 94.54 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 31 LELGYRAIDTAQIYGN-------EADIGRAIAESGVpRSELFLTTK--------VWVDNYAREKLLASLRESLEKLRTDR 95
Cdd:cd19082 27 VELGGNFIDTARVYGDwvergasERVIGEWLKSRGN-RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGTDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 96 LDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIA---AVGAGEISTNQIELS------PYLQN 166
Cdd:cd19082 106 IDLYFLHRDDP--SVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAyakAHGLPGFAASSPQWSlarpnePPWPG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 167 RALT-------AYLEEQGIAVTSYMTLAYG--------KVLKDPTLAG----------------IAARHRATVAQVALAW 215
Cdd:cd19082 184 PTLVamdeemrAWHEENQLPVFAYSSQARGffskraagGAEDDSELRRvyyseenferlerakeLAEEKGVSPTQIALAY 263
|
250 260
....*....|....*....|....*...
gi 15599362 216 AMQLGYAVIP--SSTRRENLASNLLARD 241
Cdd:cd19082 264 VLNQPFPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
2-175 |
1.75e-22 |
|
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: 93.88 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 2 SSTIHPLpSFGLGTF--RLTGQV----VVDSVRSALELGYRAIDTAQIYGN-EADIGRAIA--ESGVPRSELFLTTKV-- 70
Cdd:cd19164 10 LAGLPPL-IFGAATFsyQYTTDPesipPVDIVRRALELGIRAFDTSPYYGPsEIILGRALKalRDEFPRDTYFIITKVgr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 71 ---WVDNYAREKLLASLRESLEKLRTDRLDLVLIHwpapgnGVEL---GEYMAALAE---AKSLGLTRRIGVSNFNIE-L 140
Cdd:cd19164 89 ygpDDFDYSPEWIRASVERSLRRLHTDYLDLVYLH------DVEFvadEEVLEALKElfkLKDEGKIRNVGISGYPLPvL 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 15599362 141 TRQAIAAVGAGEISTNQIeLSpY----LQNRALTAYLEE 175
Cdd:cd19164 163 LRLAELARTTAGRPLDAV-LS-YchytLQNTTLLAYIPK 199
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
12-189 |
9.75e-22 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 91.98 E-value: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTG--------QVVVDSVRSALELGYRAIDTAQIYG---NEADIGRAIAESGvPRSELFLTTKV---WVDN--Y 75
Cdd:cd19148 8 ALGTWAIGGwmwggtdeKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKEYG-KRDRVVIATKVgleWDEGgeV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 76 AREKLLASLRE----SLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIEltrQAIAAVGAG 151
Cdd:cd19148 87 VRNSSPARIRKevedSLRRLQTDYIDLYQVHWPDPLVPIE--ETAEALKELLDEGKIRAIGVSNFSPE---QMETFRKVA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599362 152 EISTNQielSPY-LQNRA----LTAYLEEQGIAvtsymTLAYG 189
Cdd:cd19148 162 PLHTVQ---PPYnLFEREiekdVLPYARKHNIV-----TLAYG 196
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
6-257 |
1.23e-21 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 91.57 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 6 HPLPSFGLGTFRLTGQVV----------VDSVRSALELGYRAIDTAQIYG----NEAdigraIAESGVP-RSELFLTTKV 70
Cdd:PRK10376 15 RSVNRLGYGAMQLAGPGVfgppkdrdaaIAVLREAVALGVNHIDTSDFYGphvtNQL-----IREALHPyPDDLTIVTKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 71 ---------WVDNYAREKLLASLRESLEKLRTDRLDLV------LIHWPAPGNgveLGEYMAALAEAKSLGLTRRIGVSN 135
Cdd:PRK10376 90 garrgedgsWLPAFSPAELRRAVHDNLRNLGLDVLDVVnlrlmgDGHGPAEGS---IEEPLTVLAELQRQGLVRHIGLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 136 FNielTRQAIAAVGAGEIST--NQIELSpYLQNRALTAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRATVAQVAL 213
Cdd:PRK10376 167 VT---PTQVAEARKIAEIVCvqNHYNLA-HRADDALIDALARDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVAL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15599362 214 AWAMQLG--YAVIPSSTRRENLASNLLARDLRLDAEDMARIAGLER 257
Cdd:PRK10376 243 AWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIAR 288
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
24-247 |
1.50e-21 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 91.46 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 24 VDSVRSALELGYRAIDTAQIYGN---EADIGRAIaeSGVPRSELFLTTKV------WVD--NYAREKLLASLRESLEKLR 92
Cdd:cd19163 36 IRTVHEALDSGINYIDTAPWYGQgrsETVLGKAL--KGIPRDSYYLATKVgrygldPDKmfDFSAERITKSVEESLKRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 93 TDRLDLVLIHWP--APGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIaavgagEISTNQIE--LSpY----L 164
Cdd:cd19163 114 LDYIDIIQVHDIefAPSLDQILNETLPALQKLKEEGKVRFIGITGYPLDVLKEVL------ERSPVKIDtvLS-YchytL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 165 QNRALT---AYLEEQGIAVTSYMTLAYGkVLkdpTLAGIAARHRAT--------------------VAQVALAWAMQLGY 221
Cdd:cd19163 187 NDTSLLellPFFKEKGVGVINASPLSMG-LL---TERGPPDWHPASpeikeacakaaaycksrgvdISKLALQFALSNPD 262
|
250 260
....*....|....*....|....*...
gi 15599362 222 A--VIPSSTRRENLASNLLARDLRLDAE 247
Cdd:cd19163 263 IatTLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
30-252 |
2.42e-20 |
|
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: 88.65 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 30 ALELGYRAIDTAQIYG-NEADIGRAIAESGVPRSELFLTTKV-----------WVDNyAREKLLASLRESLEKLRTDRLD 97
Cdd:cd19144 43 AFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFgieknvetgeySVDG-SPEYVKKACETSLKRLGVDYID 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 98 LVLIHWPAPGNGVELgeYMAALAEAKSLGLTRRIGVSNFNIELTRQA-----IAAVgageistnQIELSPYL-----QNR 167
Cdd:cd19144 122 LYYQHRVDGKTPIEK--TVAAMAELVQEGKIKHIGLSECSAETLRRAhavhpIAAV--------QIEYSPFSldierPEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 168 ALTAYLEEQGIAVTSYMTLAYGKV---LKDPT----------------------------LAGIAARHRATVAQVALAWA 216
Cdd:cd19144 192 GVLDTCRELGVAIVAYSPLGRGFLtgaIRSPDdfeegdfrrmaprfqaenfpknlelvdkIKAIAKKKNVTAGQLTLAWL 271
|
250 260 270
....*....|....*....|....*....|....*...
gi 15599362 217 MQLGYAV--IPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19144 272 LAQGDDIipIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
7-252 |
7.70e-20 |
|
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: 86.91 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 7 PLPSFGLGTFRLTG-------QVVVDSVRSALELGYRAIDTAQIYG------NEADIGRAIAESGVPRSELFLTTKVWVD 73
Cdd:cd19077 4 LVGPIGLGLMGLTWrpnptpdEEAFETMKAALDAGSNLWNGGEFYGppdphaNLKLLARFFRKYPEYADKVVLSVKGGLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 74 NYA------REKLLASLRESLEKLR-TDRLDlvlIHWPA---PGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIElTRQ 143
Cdd:cd19077 84 PDTlrpdgsPEAVRKSIENILRALGgTKKID---IFEPArvdPNVPIE--ETIKALKELVKEGKIRGIGLSEVSAE-TIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 144 AIAAVgaGEISTNQIELSPY----LQNRALTAyLEEQGIAVTSYMTLAYG------KVLKDP------------------ 195
Cdd:cd19077 158 RAHAV--HPIAAVEVEYSLFsreiEENGVLET-CAELGIPIIAYSPLGRGlltgriKSLADIpegdfrrhldrfngenfe 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599362 196 -------TLAGIAARHRATVAQVALAWAMQLGYAVI---PSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19077 235 knlklvdALQELAEKKGCTPAQLALAWILAQSGPKIipiPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
27-252 |
9.73e-20 |
|
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: 86.90 E-value: 9.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 27 VRSALELGYRAIDTAQIYGN---EADIGRAIAESgvpRSELFLTTKV--WVDN------YAREKLLASLRESLEKLRTDR 95
Cdd:cd19091 45 VDIALDAGINFFDTADVYSEgesEEILGKALKGR---RDDVLIATKVrgRMGEgpndvgLSRHHIIRAVEASLKRLGTDY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 96 LDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNielTRQAIAAVGAGE------ISTNQIELSpyLQNR-- 167
Cdd:cd19091 122 IDLYQLHGFDALTPLE--ETLRALDDLVRQGKVRYIGVSNFS---AWQIMKALGISErrglarFVALQAYYS--LLGRdl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 168 --ALTAYLEEQGIAVTSYMTLAY----GKVLKD----------------------------PTLAGIAARHRATVAQVAL 213
Cdd:cd19091 195 ehELMPLALDQGVGLLVWSPLAGgllsGKYRRGqpapegsrlrrtgfdfppvdrergydvvDALREIAKETGATPAQVAL 274
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599362 214 AWAMQLGY--AVIPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19091 275 AWLLSRPTvsSVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
12-170 |
5.39e-19 |
|
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: 84.51 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTGQ--------VVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESGVPRSELFLTTKV-----WVDNY 75
Cdd:cd19153 16 GLGTAALGGVygdgleqdEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVgryrdSEFDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 76 AREKLLASLRESLEKLRTDRLDLVLIHwpapgnGVELGEY-------MAALAEAKSLGLTRRIGVSNFNIELTRQAIAAV 148
Cdd:cd19153 96 SAERVRASVATSLERLHTTYLDVVYLH------DIEFVDYdtlvdeaLPALRTLKDEGVIKRIGIAGYPLDTLTRATRRC 169
|
170 180
....*....|....*....|..
gi 15599362 149 GAGEISTNQIELSPYLQNRALT 170
Cdd:cd19153 170 SPGSLDAVLSYCHLTLQDARLE 191
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
27-252 |
9.74e-19 |
|
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: 83.82 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 27 VRSALELGYRAIDTAQIYG---NEADIGRAIAEsgvPRSELFLTTKVWVD-----------NYAREKLLASLRESLEKLR 92
Cdd:cd19078 31 IRKAVELGITFFDTAEVYGpytNEELVGEALKP---FRDQVVIATKFGFKidggkpgplglDSRPEHIRKAVEGSLKRLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 93 TDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQA-----IAAVgageistnQIELSpyLQNR 167
Cdd:cd19078 108 TDYIDLYYQHRVDP--NVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAhavcpVTAV--------QSEYS--MMWR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 168 ----ALTAYLEEQGIAVTSYMTLAYG----KVLKDPT---------------------------LAGIAARHRATVAQVA 212
Cdd:cd19078 176 epekEVLPTLEELGIGFVPFSPLGKGfltgKIDENTKfdegddraslprftpealeanqalvdlLKEFAEEKGATPAQIA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15599362 213 LAWAM-QLGYAV-IPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19078 256 LAWLLaKKPWIVpIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-219 |
1.10e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 82.96 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 11 FGL--GTFRLTGQVVVDSVRS----ALELGYRAIDTAQIYGN-EADIGRAIAESgvprSELFLTTKV----WVDNYAREK 79
Cdd:cd19097 10 FGLdyGIANKSGKPSEKEAKKileyALKAGINTLDTAPAYGDsEKVLGKFLKRL----DKFKIITKLpplkEDKKEDEAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 80 LLASLRESLEKLRTDRLDLVLIHWPA--PGNGvelGEYMAALAEAKSLGLTRRIGVSNFNIEltrQAIAAVGAGEISTNQ 157
Cdd:cd19097 86 IEASVEASLKRLKVDSLDGLLLHNPDdlLKHG---GKLVEALLELKKEGLIRKIGVSVYSPE---ELEKALESFKIDIIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 158 IELSPY---LQNRALTAYLEEQGIAV------------------TSYMTLAYGKVLKdptLAGIAARHRATVAQVALAWA 216
Cdd:cd19097 160 LPFNILdqrFLKSGLLAKLKKKGIEIharsvflqglllmepdklPAKFAPAKPLLKK---LHELAKKLGLSPLELALGFV 236
|
...
gi 15599362 217 MQL 219
Cdd:cd19097 237 LSL 239
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-241 |
2.82e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 82.38 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 31 LELGYRAIDTAQIYG----------NEADIGRAIAESGVpRSELFLTTKV---------WVDNY---AREKLLASLRESL 88
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGRWLKDRGN-RDDVVIATKVgagprdpdgGPESPeglSAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 89 EKLRTDRLDLVLIHWPAPGngVELGEYMAALAEAKSLGLTRRIGVSNF---NIELTRQAIAAVGAGEISTNQIELSpYLQ 165
Cdd:cd19752 106 RRLGTDYIDLYYAHVDDRD--TPLEETLEAFNELVKAGKVRAIGASNFaawRLERARQIARQQGWAEFSAIQQRHS-YLR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 166 NRA-------------LTAYLEEQG-IAVTSYMTLAYG------KVLKDP-----------TLAGIAARHRATVAQVALA 214
Cdd:cd19752 183 PRPgadfgvqrivtdeLLDYASSRPdLTLLAYSPLLSGaytrpdRPLPEQydgpdsdarlaVLEEVAGELGATPNQVVLA 262
|
250 260
....*....|....*....|....*....
gi 15599362 215 WAMQLGYAVIP--SSTRRENLASNLLARD 241
Cdd:cd19752 263 WLLHRTPAIIPllGASTVEQLEENLAALD 291
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
12-247 |
7.08e-18 |
|
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: 81.10 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTGQVVVDS-----VRSALELGYRAIDTAQIYGN---EADIGRAIAesGVPRSELFLTTKV------WVDNY-- 75
Cdd:cd19074 8 SLGTWLTFGGQVDDEdakacVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfwptgpGPNDRgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 76 AREKLLASLRESLEKLRTDRLDLVLIHWPAPgnGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQA---IAAVGAGE 152
Cdd:cd19074 86 SRKHIFESIHASLKRLQLDYVDIYYCHRYDP--ETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAhdlARQFGLIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 153 ISTNQIELSpYLQNRA---LTAYLEEQGIAVTSYMTLAYG-------------------------------------KVL 192
Cdd:cd19074 164 PVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkrrlltdenleKVK 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599362 193 KdptLAGIAARHRATVAQVALAWAMQ--LGYAVIPSSTRRENLASNLLARDLRLDAE 247
Cdd:cd19074 243 K---LKPIADELGLTLAQLALAWCLRnpAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-237 |
3.51e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 79.67 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 10 SFGLGTFRL-----TGQVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAES----GVPRSELFLTTKV------- 70
Cdd:cd19099 5 SLGLGTYRGdsddeTDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELiekgGIKRDEVVIVTKAgyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 71 --------WVDNYAREKLL------------------ASLRESLEKLRTDRLDLVLIHWP------APGNGV--ELGEYM 116
Cdd:cd19099 85 deplrplkYLEEKLGRGLIdvadsaglrhcispayleDQIERSLKRLGLDTIDLYLLHNPeeqlleLGEEEFydRLEEAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 117 AALAEAKSLGLTRRIGVS-----------NFNIELTRQAIAAVGAG---------EISTNQIELSPYL-------QNRAL 169
Cdd:cd19099 165 EALEEAVAEGKIRYYGIStwdgfrappalPGHLSLEKLVAAAEEVGgdnhhfkviQLPLNLLEPEALTekntvkgEALSL 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599362 170 TAYLEEQGIAVTSYMTLAYGKVLKDPTLAGIAARHRA-TVAQVALAWA-MQLGY-AVIPSSTRRENLASNL 237
Cdd:cd19099 245 LEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGaTLAQRALQFArSTPGVdSALVGMRRPEHVDENL 315
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-252 |
5.55e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 78.91 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 30 ALELGYRAIDTAQIYG---NEADIGRAIAEsgVPRSELFLTTK---VWVDNYArEKLLASLRESLEKLRTDRLDLVLIHW 103
Cdd:cd19103 41 AMAAGLNLWDTAAVYGmgaSEKILGEFLKR--YPREDYIISTKftpQIAGQSA-DPVADMLEGSLARLGTDYIDIYWIHN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 104 PA--PGNGVELgeymAALAEAkslGLTRRIGVSNFNIELTRQAIAAVGAGEISTNQIELSPYLQNRA-----LTAYLEEQ 176
Cdd:cd19103 118 PAdvERWTPEL----IPLLKS---GKVKHVGVSNHNLAEIKRANEILAKAGVSLSAVQNHYSLLYRSseeagILDYCKEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 177 GIAVTSYMTL-----------------------AYGKVLKD-----PTLAGIAARHRATVAQVALAWAMQLGYAVIPSST 228
Cdd:cd19103 191 GITFFAYMVLeqgalsgkydtkhplpegsgraeTYNPLLPQleeltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVT 270
|
250 260
....*....|....*....|....
gi 15599362 229 RRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19103 271 KPHHVEDAARAASITLTDDEIKEL 294
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
38-252 |
4.47e-16 |
|
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: 76.49 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 38 IDTAQIYGN---EADIGRAIAESgvpRSELFLTTK-VWVDNYA--------REKLLASLRESLEKLRTDRLDLVLIHWPA 105
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAGN---RDRIVLATKyTMNRRPGdpnaggnhRKNLRRSVEASLRRLQTDYIDLLYVHAWD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 106 PGNGVElgEYMAALAEAKSLGLTRRIGVSNFN--IELTRQAIA-AVGAGEISTNQIELSpyLQNRA----LTAYLEEQGI 178
Cdd:cd19080 125 FTTPVE--EVMRALDDLVRAGKVLYVGISDTPawVVARANTLAeLRGWSPFVALQIEYS--LLERTpereLLPMARALGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 179 AVTSYMTLAYGK-----------------------VLKDP-------TLAGIAARHRATVAQVALAWAMQLGYAVIPS-- 226
Cdd:cd19080 201 GVTPWSPLGGGLltgkyqrgeegrageakgvtvgfGKLTErnwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVIPIig 280
|
250 260
....*....|....*....|....*.
gi 15599362 227 STRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19080 281 ARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
11-216 |
4.51e-16 |
|
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: 75.68 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 11 FGLGTFRLTG--------QVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAEsgVPRSELFLTTK--VWVDNyAR 77
Cdd:cd19096 3 LGFGTMRLPEsdddsideEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKlpPWSVK-SA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 78 EKLLASLRESLEKLRTDRLDLVLIHWP---------APGNGVElgeymaALAEAKSLGLTRRIGVSnF--NIELTRQAIA 146
Cdd:cd19096 80 EDFRRILEESLKRLGVDYIDFYLLHGLnspewlekaRKGGLLE------FLEKAKKEGLIRHIGFS-FhdSPELLKEILD 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599362 147 avgAGEISTNQIELS----PYLQNRALTAYLEEQGIAVTSYMTLAYGKVLKDPT-LAGIAARHRATVAQVALAWA 216
Cdd:cd19096 153 ---SYDFDFVQLQYNyldqENQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPeALAILCGAPLSPAEWALRFL 224
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
8-250 |
6.84e-16 |
|
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: 75.76 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTG-----QVVVDSVRSALELGYRAIDTAQIYGN-----EADIGRAIAESGVP-RSELFLTTKV----WV 72
Cdd:cd19089 11 LPAISLGLWHNFGdytspEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRPyRDELVISTKAgygmWP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 73 DNYA----REKLLASLRESLEKLRTDRLDLVLIHWPAPGngVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIA-- 146
Cdd:cd19089 91 GPYGdggsRKYLLASLDQSLKRMGLDYVDIFYHHRYDPD--TPLEETMTALADAVRSGKALYVGISNYPGAKARRAIAll 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 147 -AVGAgEISTNQIELSpyLQNR----ALTAYLEEQGIAVTSYMTLAYG----KVLKDP---------------------- 195
Cdd:cd19089 169 rELGV-PLIIHQPRYS--LLDRwaedGLLEVLEEAGIGFIAFSPLAQGlltdKYLNGIppdsrraaeskflteealtpek 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599362 196 -----TLAGIAARHRATVAQVALAWAMQLGY--AVIPSSTRRENLASNLLARD-LRLDAEDMA 250
Cdd:cd19089 246 leqlrKLNKIAAKRGQSLAQLALSWVLRDPRvtSVLIGASSPSQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
11-136 |
6.84e-16 |
|
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: 75.67 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 11 FGLGTF-RLTGQVVVDSVRSAL----ELGYRAIDTAQIYGN---EADIGRAiaesGVPRSELFLTTKV---WVDNYAREK 79
Cdd:cd19075 5 LGTMTFgSQGRFTTAEAAAELLdaflERGHTEIDTARVYPDgtsEELLGEL----GLGERGFKIDTKAnpgVGGGLSPEN 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599362 80 LLASLRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNF 136
Cdd:cd19075 81 VRKQLETSLKRLKVDKVDVFYLHAPDRSTPLE--ETLAAIDELYKEGKFKEFGLSNY 135
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
30-252 |
7.41e-14 |
|
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: 70.29 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 30 ALELGYRAIDTAQIY---------G-NEADIGRAIAESGvPRSELFLTTKV--------WVD----NYAREKLLASLRES 87
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqGrTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPRgggtRLDRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPA----------------PGNGVELGEYMAALAEAKSLGLTRRIGVSN---FNI-ELTRQAIAA 147
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPDrytplfgggyytepseEEDSVSFEEQLEALGELVKAGKIRHIGLSNetpWGVmKFLELAEQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 148 --------------------VGAGEIST-NQIELSPY--LQNRALTA-YLEEQGIAVTSYMTL--AYGKVLKDPT----- 196
Cdd:cd19094 186 glprivsiqnpysllnrnfeEGLAEACHrENVGLLAYspLAGGVLTGkYLDGAARPEGGRLNLfpGYMARYRSPQaleav 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 197 --LAGIAARHRATVAQVALAWAMQLGY--AVIPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19094 266 aeYVKLARKHGLSPAQLALAWVRSRPFvtSTIIGATTLEQLKENIDAFDVPLSDELLAEI 325
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
8-218 |
8.05e-14 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 70.12 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQV-VVDS----VRSALELGYRAIDTAQIYG-----NEADIGRAIAESGVP-RSELFLTTK----VWV 72
Cdd:cd19151 12 LPAISLGLWHNFGDVdRYENsramLRRAFDLGITHFDLANNYGpppgsAEENFGRILKEDLKPyRDELIISTKagytMWP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 73 DNY----AREKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAV 148
Cdd:cd19151 92 GPYgdwgSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLE--ETMGALDQIVRQGKALYVGISNYPPEEAREAAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 149 gaGEIST----NQIELSpyLQNRA----LTAYLEEQGIAVTSYMTLAYGkVLKDPTLAGIAARHRA-------------- 206
Cdd:cd19151 170 --KDLGTpcliHQPKYS--MFNRWveegLLDVLEEEGIGCIAFSPLAQG-LLTDRYLNGIPEDSRAakgssflkpeqite 244
|
250 260 270
....*....|....*....|....*....|
gi 15599362 207 ------------------TVAQVALAWAMQ 218
Cdd:cd19151 245 eklakvrrlneiaqargqKLAQMALAWVLR 274
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
8-252 |
2.92e-13 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 68.86 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTGQV-VVDS----VRSALELGYRAIDTAQIYG-----NEADIGRAIAESGVP-RSELFLTTK----VWV 72
Cdd:PRK09912 25 LPALSLGLWHNFGHVnALESqraiLRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagydMWP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 73 DNY----AREKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAV 148
Cdd:PRK09912 105 GPYgsggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPME--ETASALAHAVQSGKALYVGISSYSPERTQKMVELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 149 GAGEISTNQIELSPYLQNR-----ALTAYLEEQGIAVTSYMTLAYG----------------------------KVLKDP 195
Cdd:PRK09912 183 REWKIPLLIHQPSYNLLNRwvdksGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpKMLTEA 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599362 196 TLAGI------AARHRATVAQVALAWAMQLG--YAVIPSSTRRENLASNLLA-RDLRLDAEDMARI 252
Cdd:PRK09912 263 NLNSLrllnemAQQRGQSMAQMALSWLLKDErvTSVLIGASRAEQLEENVQAlNNLTFSTEELAQI 328
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-147 |
3.85e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 68.06 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 10 SFGLGTfrlTGQVVVDS--------VRSALELGYRAIDTAQIYGN---EADIGRAIAESgvpRSELFLTTKVWVDNYARE 78
Cdd:cd19104 16 TFGGGG---IGGLMGRTtreeqiaaVRRALDLGINFFDTAPSYGDgksEENLGRALKGL---PAGPYITTKVRLDPDDLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 79 KLLASLRESLEK----LRTDRLDLVLIH--------WPAPGNG-----VELGEYMAALAEAKSLGLTRRIGVSNF-NIEL 140
Cdd:cd19104 90 DIGGQIERSVEKslkrLKRDSVDLLQLHnrigderdKPVGGTLsttdvLGLGGVADAFERLRSEGKIRFIGITGLgNPPA 169
|
....*..
gi 15599362 141 TRQAIAA 147
Cdd:cd19104 170 IRELLDS 176
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
12-252 |
5.89e-13 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 67.46 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTG--------QVVVDSVRSALELGYRAIDTAQIYG---NEADIGRAIaeSGVPRSELFLTTKVWVDNYAREKL 80
Cdd:cd19145 16 GLGCMGLSGdygapkpeEEGIALIHHAFNSGVTFLDTSDIYGpntNEVLLGKAL--KDGPREKVQLATKFGIHEIGGSGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 81 L---------ASLRESLEKLRTDRLDLVLIHwpAPGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAvgaG 151
Cdd:cd19145 94 EvrgdpayvrAACEASLKRLDVDYIDLYYQH--RIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAV---H 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 152 EISTNQIELSPYlqnralTAYLEEQ--------GIAVTSYMTLAYG------KVLKDPT--------------------- 196
Cdd:cd19145 169 PITAVQLEWSLW------TRDIEEEiiptcrelGIGIVPYSPLGRGffagkaKLEELLEnsdvrkshprfqgenleknkv 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599362 197 ----LAGIAARHRATVAQVALAWAMQLGYAV--IPSSTRRENLASNLLARDLRLDAEDMARI 252
Cdd:cd19145 243 lyerVEALAKKKGCTPAQLALAWVLHQGEDVvpIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
30-255 |
1.48e-12 |
|
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: 66.44 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 30 ALELGYRAIDTAQIYGN---EADIGRAIAESgvpRSELFLTTKV--------WVDNYAREKLLASLRESLEKLRTDRLDL 98
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKVfgpmgddpNDRGLSRRHIRRAVEASLRRLQTDYIDL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 99 VLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNF---NIElTRQAIAAVG--AGEIStnqiELSPY-LQNRalTAY 172
Cdd:cd19087 116 YQMHHFDRDTPLE--ETLRALDDLVRQGKIRYIGVSNFaawQIA-KAQGIAARRglLRFVS----EQPMYnLLKR--QAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 173 LE------EQGIAVTSYMTLA-------YGKVLKDPT------------------------LAGIAARHRATVAQVALAW 215
Cdd:cd19087 187 LEilpaarAYGLGVIPYSPLAgglltgkYGKGKRPESgrlveraryqarygleeyrdiaerFEALAAEAGLTPASLALAW 266
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15599362 216 AMQ---LGYAVIPSSTrRENLASNLLARDLRLDAEDMARIAGL 255
Cdd:cd19087 267 VLShpaVTSPIIGPRT-LEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
9-218 |
3.04e-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: 65.07 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 9 PSFGLGT------FRLTGQVVVDSVRSALELGYRAIDTAQIYG---NEADIGRAIAesGVPRSELFLTTKV--------- 70
Cdd:cd19162 1 PRLGLGAaslgnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 71 -------WVDNYAREKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVELGEYMAALAEAKSLGLTRRIGVSNFNIELTRQ 143
Cdd:cd19162 79 grpagadRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 144 AIAAVG------AGEIStnqielspYLQNRALTAYLE---EQGIAVTSYMTLAYGKVLKDPT------------------ 196
Cdd:cd19162 159 AARRADvdvvmvAGRYT--------LLDRRAATELLPlcaAKGVAVVAAGVFNSGILATDDPagdrydyrpatpevlara 230
|
250 260
....*....|....*....|....
gi 15599362 197 --LAGIAARHRATVAQVALAWAMQ 218
Cdd:cd19162 231 rrLAAVCRRYGVPLPAAALQFPLR 254
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
8-250 |
1.59e-11 |
|
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: 63.24 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTFRLTG-----QVVVDSVRSALELGYRAIDTAQIYG-----NEADIGRAIAESGVP-RSELFLTTK----VWV 72
Cdd:cd19150 12 LPALSLGLWHNFGddtplETQRAILRTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAGyRDELIISTKagydMWP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 73 DNY----AREKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAV 148
Cdd:cd19150 92 GPYgewgSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLE--ETMGALDHAVRSGKALYVGISSYSPERTREAAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 149 GAGEI-------STNQieLSPYLQNRALTAYLEEQGIAVTSYMTLAYGkVLKDPTLAGIAARHRA--------------- 206
Cdd:cd19150 170 RELGTpllihqpSYNM--LNRWVEESGLLDTLQELGVGCIAFTPLAQG-LLTDKYLNGIPEGSRAskerslspkmltean 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599362 207 ----------------TVAQVALAWAMQLG--YAVIPSSTRRENLASNLLARD-LRLDAEDMA 250
Cdd:cd19150 247 lnsiralneiaqkrgqSLAQMALAWVLRDGrvTSALIGASRPEQLEENVGALDnLTFSADELA 309
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
24-189 |
3.55e-11 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 62.49 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 24 VDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESGVPRSELFLTTKV--WVD--NYAREKLLASLRESLEKLRTDRL 96
Cdd:PLN02587 34 IASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCgrYGEgfDFSAERVTKSVDESLARLQLDYV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 97 DLVLIHwpapgnGVELG-------EYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVGAGEIS------------TNQ 157
Cdd:PLN02587 114 DILHCH------DIEFGsldqivnETIPALQKLKESGKVRFIGITGLPLAIFTYVLDRVPPGTVDvilsychyslndSSL 187
|
170 180 190
....*....|....*....|....*....|..
gi 15599362 158 IELSPYLQNRaltayleeqGIAVTSYMTLAYG 189
Cdd:PLN02587 188 EDLLPYLKSK---------GVGVISASPLAMG 210
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
30-257 |
2.09e-10 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 60.25 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 30 ALELGYRAIDTAQIYG----------NEADIGRAIAESGvPRSELFLTTKV----------WVDNYA--REKLLASLRES 87
Cdd:PRK10625 39 AVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVsgpsrnndkgIRPNQAldRKNIREALHDS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 88 LEKLRTDRLDLVLIHWPA-PGN--------------GVELGEYMAALAEAKSLGLTRRIGVSN---FNIELTRQAIAAVG 149
Cdd:PRK10625 118 LKRLQTDYLDLYQVHWPQrPTNcfgklgyswtdsapAVSLLETLDALAEQQRAGKIRYIGVSNetaFGVMRYLHLAEKHD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 150 AGEISTNQielSPY-LQNRALTAYLEE----QGIAVTSYMTLAYG----KVLKDPTLAG--------------------- 199
Cdd:PRK10625 198 LPRIVTIQ---NPYsLLNRSFEVGLAEvsqyEGVELLAYSCLAFGtltgKYLNGAKPAGarntlfsrftrysgeqtqkav 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599362 200 -----IAARHRATVAQVALAWAMQLGY--AVIPSSTRRENLASNLLARDLRLDAEDMARIAGLER 257
Cdd:PRK10625 275 aayvdIAKRHGLDPAQMALAFVRRQPFvaSTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
27-237 |
2.55e-09 |
|
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: 56.85 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 27 VRSALELGYRAIDTAQIYGN---EADIGRAIAEsgVPRSELFLTTKV------------------WVD-------NYARE 78
Cdd:cd19152 26 LVAAWDLGIRYFDTAPWYGAglsEERLGAALRE--LGREDYVISTKVgrllvplqeveptfepgfWNPlpfdavfDYSYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 79 KLLASLRESLEKLRTDRLDLVLIHWPAPGNGVE---------LGEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIAAVG 149
Cdd:cd19152 104 GILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAesdehfaqaIKGAFRALEELREEGVIKAIGLGVNDWEVILRILEEAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 150 ------AGeiSTNQIELSPYlqnRALTAYLEEQGIAV--------------TSYMTLAYGKVlkDP-------TLAGIAA 202
Cdd:cd19152 184 ldwvmlAG--RYTLLDHSAA---RELLPECEKRGVKVvnagpfnsgflaggDNFDYYEYGPA--PPeliarrdRIEALCE 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 15599362 203 RHRATVAQVALAWAMQ--LGYAVIPSSTRRENLASNL 237
Cdd:cd19152 257 QHGVSLAAAALQFALAppAVASVAPGASSPERVEENV 293
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
20-252 |
6.01e-09 |
|
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: 55.68 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 20 GQVVVDSVRSALELGYRA----IDTAQIYGN---EADIGRAIAESGVPRSELFLTTKV-WVDN--------YAREKLLAS 83
Cdd:cd19143 26 NQVDVDEAKECMKAAYDAgvnfFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWGGGgpppndrgLSRKHIVEG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 84 LRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIELTRQAIA-AVGAGEI--STNQIEL 160
Cdd:cd19143 106 TKASLKRLQLDYVDLVFCHRPDPATPIE--ETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEiADRLGLIppVMEQPQY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 161 SPYLQNRALTAYL---EEQGIAVTSYMTLAYG---------------------KVLKDPT-------------LAGIAAR 203
Cdd:cd19143 184 NLFHRERVEVEYAplyEKYGLGTTTWSPLASGlltgkynngipegsrlalpgyEWLKDRKeelgqekiekvrkLKPIAEE 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15599362 204 HRATVAQVALAWAMQLGY--AVIPSSTRRENLASNLLARDL--RLDAEDMARI 252
Cdd:cd19143 264 LGCSLAQLAIAWCLKNPNvsTVITGATKVEQLEENLKALEVlpKLTPEVMEKI 316
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-255 |
8.56e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 52.35 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 29 SALELGYRAIDTAQIYGN-EADIGRAIAESGVPRSELFLTTKvW----------------VDNYAREKLLASLRESLEKL 91
Cdd:cd19098 43 AAWAAGVRYFDAARSYGRaEEFLGSWLRSRNIAPDAVFVGSK-WgytytadwqvdaavheVKDHSLARLLKQWEETRSLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 92 rTDRLDLVLIHWPAPGNGV-ELGEYMAALAEAKSLGltRRIGVSnfnIELTRQAIAAVGAGEISTNQIELSPYLQ----- 165
Cdd:cd19098 122 -GKHLDLYQIHSATLESGVlEDADVLAALAELKAEG--VKIGLS---LSGPQQAETLRRALEIEIDGARLFDSVQatwnl 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 166 --NRALTAYLE--EQGIAVTSYMTLAYGKVLKDPT----------LAGIAARHRATVAQVALAWAMQLGYA--VIPSSTR 229
Cdd:cd19098 196 leQSAGEALEEahEAGMGVIVKEALANGRLTDRNPspelaplmavLKAVADRLGVTPDALALAAVLAQPFVdvVLSGAAT 275
|
250 260
....*....|....*....|....*.
gi 15599362 230 RENLASNLLARDLRLDAEDMARIAGL 255
Cdd:cd19098 276 PEQLRSNLRALDVSLDLELLAALADL 301
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
9-102 |
1.03e-07 |
|
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: 51.94 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 9 PSFGLGTFRLTG-------QVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAEsgVPRSELFLTTKV-------- 70
Cdd:cd19161 1 SELGLGTAGLGNlytavsnADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKVgrllkpar 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15599362 71 ---------WVD--------NYAREKLLASLRESLEKLRTDRLDLVLIH 102
Cdd:cd19161 79 egsvpdpngFVDplpfeivyDYSYDGIMRSFEDSLQRLGLNRIDILYVH 127
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
8-102 |
3.98e-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: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 8 LPSFGLGTF-----RLTGQVVVDSVRSALELGYRAIDTAQIYGN---EADIGRAIAESGVPRSELFLTTKVWVDN----- 74
Cdd:cd19142 13 VSNVGLGTWstfstAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIYWSYgseer 92
|
90 100
....*....|....*....|....*....
gi 15599362 75 -YAREKLLASLRESLEKLRTDRLDLVLIH 102
Cdd:cd19142 93 gLSRKHIIESVRASLRRLQLDYIDIVIIH 121
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
12-111 |
5.41e-06 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 46.67 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTF-----RLTGQVVVDSVRSALELGYRAIDTAQIY-GNEADI--GRAIAESGVPRSELFLTTKVWVDNYA------- 76
Cdd:cd19141 16 GLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYaAGKAEIvlGKILKKKGWRRSSYVITTKIFWGGKAetergls 95
|
90 100 110
....*....|....*....|....*....|....*
gi 15599362 77 REKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVE 111
Cdd:cd19141 96 RKHIIEGLKASLERLQLEYVDIVFANRPDPNTPME 130
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
11-137 |
5.46e-06 |
|
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: 47.00 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 11 FGLGTFRLTGQVVVDSVRSAL-----ELGYRAIDTAQIYGN---EADIGRAIAESGVPRSELFLTTKVWVDNYA------ 76
Cdd:cd19158 16 LGLGTWVTFGGQITDEMAEHLmtlayDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIFWGGKAetergl 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599362 77 -REKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFN 137
Cdd:cd19158 96 sRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPME--ETVRAMTHVINQGMAMYWGTSRWS 155
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
32-252 |
1.55e-05 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 45.59 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 32 ELGYRAIDTAQIYGNEAD---IGRAIAESGVpRSELFLTTKVWVD------------NYA---REKLLASLRESLEKLRT 93
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFTTDykayevgkgkavNYCgnhKRSLHVSVRDSLRKLQT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 94 DRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNfnieltRQAIAAVGAGEISTNQ--IELSPYlQNR--AL 169
Cdd:cd19147 124 DWIDILYVHWWDYTTSIE--EVMDSLHILVQQGKVLYLGVSD------TPAWVVSAANYYATAHgkTPFSVY-QGRwnVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 170 TAYLEEQ--------GIAVTSYMTLAYGKVLKDPT------------------------------LAGIAARH-RATVAQ 210
Cdd:cd19147 195 NRDFERDiipmarhfGMALAPWDVLGGGKFQSKKAveerkkngeglrsfvggteqtpeevkiseaLEKVAEEHgTESVTA 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15599362 211 VALAWAMQLGYAVIPSSTRR--ENLASNLLARDLRLDAEDMARI 252
Cdd:cd19147 275 IALAYVRSKAPNVFPLVGGRkiEHLKDNIEALSIKLTPEEIEYL 318
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
11-137 |
1.70e-05 |
|
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: 45.42 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 11 FGLGTFRLTGQVVVDSVRS-----ALELGYRAIDTAQIYGN---EADIGRAIAESGVPRSELFLTTKVWVDNYA------ 76
Cdd:cd19159 16 LGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLYWGGKAetergl 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599362 77 -REKLLASLRESLEKLRTDRLDLVLIHwpAPGNGVELGEYMAALAEAKSLGLTRRIGVSNFN 137
Cdd:cd19159 96 sRKHIIEGLKGSLQRLQLEYVDVVFAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS 155
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
12-137 |
3.85e-05 |
|
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: 44.21 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 12 GLGTFRLTGQVVVDSVRS-----ALELGYRAIDTAQIYGN---EADIGRAIAESGVPRSELFLTTKVWVDNYA------- 76
Cdd:cd19160 19 GLGTWVTFGSQISDETAEdlltvAYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWRRSSYVVTTKIYWGGQAetergls 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599362 77 REKLLASLRESLEKLRTDRLDLVLIHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFN 137
Cdd:cd19160 99 RKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPME--EIVRAMTYVINQGMAMYWGTSRWS 157
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
38-252 |
2.51e-03 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 38.56 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 38 IDTAQIY---GNEADIGRAIAESGVpRSELFLTTKVWVD-----------NYA---REKLLASLRESLEKLRTDRLDLVL 100
Cdd:cd19146 52 IDTANNYqgeESERWVGEWMASRGN-RDEMVLATKYTTGyrrggpikiksNYQgnhAKSLRLSVEASLKKLQTSYIDILY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 101 IHWPAPGNGVElgEYMAALAEAKSLGLTRRIGVSNFNIELT------------RQAIAAVGAGEISTNQIE--------- 159
Cdd:cd19146 131 VHWWDYTTSIP--ELMQSLNHLVAAGKVLYLGVSDTPAWVVskanayarahglTQFVVYQGHWSAAFRDFErdilpmcea 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599362 160 ----LSPY---LQNRALTAYLEEQGIAVTSYM---TLAYGKVLKdpTLAGIAARHRATVAQVALAWAMQLGYAVIPSSTR 229
Cdd:cd19146 209 egmaLAPWgvlGQGQFRTEEEFKRRGRSGRKGgpqTEKERKVSE--KLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGG 286
|
250 260
....*....|....*....|....*
gi 15599362 230 R--ENLASNLLARDLRLDAEDMARI 252
Cdd:cd19146 287 RkvEHLKGNIEALGISLSDEEIQEI 311
|
|
| |
