|
Name |
Accession |
Description |
Interval |
E-value |
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-346 |
0e+00 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 773.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVPPRPETQGLTETYVGNWLAKHGSRE 80
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRPETQGLTETYIGNWLAKRGSRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 81 KLIVASKVSGPSRNNDSGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYSWTDSAPVVSLLDT 160
Cdd:PRK10625 81 KLIIASKVSGPSRNNDKGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYSWTDSAPAVSLLET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 161 LDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGT 240
Cdd:PRK10625 161 LDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 241 LTGKYLNGAKPAGARNTLFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVE 320
Cdd:PRK10625 241 LTGKYLNGAKPAGARNTLFSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIE 320
|
330 340
....*....|....*....|....*.
gi 2551249852 321 SLHLELSEEVLAEIEAVHQVYTYPAP 346
Cdd:PRK10625 321 SLHLTLSEEVLAEIEAVHQVYTYPAP 346
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-337 |
0e+00 |
|
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: 545.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 13 VSTLGLGTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVPPRPETQGLTETYVGNWLAKHGSREKLIVASKVSGPS 92
Cdd:cd19094 1 VSEICLGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPSPETQGRTEEIIGSWLKKKGNRDKVVLATKVAGPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 93 RNNDSGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYS-WTDSAPVVSLLDTLDALAEFQRAG 171
Cdd:cd19094 81 EGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLFGGGYYTePSEEEDSVSFEEQLEALGELVKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 172 KIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYLNGA-K 250
Cdd:cd19094 161 KIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAaR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 251 PAGARNTLFSRF-TRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHLELSEE 329
Cdd:cd19094 241 PEGGRLNLFPGYmARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVPLSDE 320
|
....*...
gi 2551249852 330 VLAEIEAV 337
Cdd:cd19094 321 LLAEIDAV 328
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-344 |
8.93e-123 |
|
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: 355.64 E-value: 8.93e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTMTFGE---QNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetQGLTETYVGNWLAKHg 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYG-------PGRSEELLGEALKGR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 78 SREKLIVASKVSGPSRNNDSGIRpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSL 157
Cdd:COG0667 73 PRDDVVIATKVGRRMGPGPNGRG----LSREHIRRAVEASLRRLGTDYIDLYQLHRPD-----------------PDTPI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 158 LDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADkhDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLG 237
Cdd:COG0667 132 EETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 238 FGTLTGKYLNGAK-PAGARNTLFsRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLK 316
Cdd:COG0667 210 GGLLTGKYRRGATfPEGDRAATN-FVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLE 288
|
330 340
....*....|....*....|....*...
gi 2551249852 317 TNVESLHLELSEEVLAEIEAVHQVYTYP 344
Cdd:COG0667 289 ENLAAADLELSAEDLAALDAALAAVPAP 316
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-337 |
6.07e-95 |
|
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: 284.85 E-value: 6.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetQGLTETYVGNWLAKHgsRE 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYG-------GGRSEEIIGRWIAGR--RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 81 KLIVASKVSGP--SRNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsapvvSLL 158
Cdd:cd19087 72 DIVLATKVFGPmgDDPNDRG------LSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDT-----------------PLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 159 DTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGF 238
Cdd:cd19087 129 ETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 239 GTLTGKYLNGAKPAGARNTLFSRFT-RYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKT 317
Cdd:cd19087 209 GLLTGKYGKGKRPESGRLVERARYQaRYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLED 288
|
330 340
....*....|....*....|
gi 2551249852 318 NVESLHLELSEEVLAEIEAV 337
Cdd:cd19087 289 SLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
8-334 |
2.68e-91 |
|
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: 275.25 E-value: 2.68e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 8 HSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVPPRPETQGLTETYVGNWLAKHGSREKLIVASK 87
Cdd:cd19081 4 RTGLSVSPLCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPGNAGGESETIIGRWLKSRGKRDRVVIATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 88 VSGPSRNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLDTLDALAEF 167
Cdd:cd19081 84 VGFPMGPNGPG------LSRKHIRRAVEASLRRLQTDYIDLYQAHWDD-----------------PATPLEETLGALNDL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 168 QRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNR-SFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYL 246
Cdd:cd19081 141 IRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDReSFEGELLPLCREEGIGVIPYSPLAGGFLTGKYR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 247 NGAKPAGARNTlFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHLEL 326
Cdd:cd19081 221 SEADLPGSTRR-GEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRL 299
|
....*...
gi 2551249852 327 SEEVLAEI 334
Cdd:cd19081 300 TDEEVARL 307
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-335 |
1.17e-82 |
|
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: 252.83 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 10 SLEVSTLGLGTMTFG--------EQNSEADAHAQLDyavvQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAkhGSREK 81
Cdd:cd19084 1 DLKVSRIGLGTWAIGgtwwgevdDQESIEAIKAAID----LGINFFDTAPVY-------GFGHSEEILGKALK--GRRDD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 82 LIVASKVsGPSRNNDSGIRPNqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLDTL 161
Cdd:cd19084 68 VVIATKC-GLRWDGGKGVTKD--LSPESIRKEVEQSLRRLQTDYIDLYQIHWPD-----------------PNTPIEETA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 162 DALAEFQRAGKIRYIGVSNETAFGVMRYLHLADkhdlprIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTL 241
Cdd:cd19084 128 EALEKLKKEGKIRYIGVSNFSVEQLEEARKYGP------IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 242 TGKYLNGAK--PAGARNTlFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNV 319
Cdd:cd19084 202 TGKYKKEPTfpPDDRRSR-FPFFRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENA 280
|
330
....*....|....*.
gi 2551249852 320 ESLHLELSEEVLAEIE 335
Cdd:cd19084 281 GALDWELTEEELKEID 296
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-337 |
9.29e-81 |
|
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: 248.68 E-value: 9.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTMTFGEQN---------SEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGN 71
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGgffgawggvDQEEADRLVDIALDAGINFFDTADVY-------SEGESEEILGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 72 WLAkhGSREKLIVASKVSGPSRN--NDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswt 149
Cdd:cd19091 74 ALK--GRRDDVLIATKVRGRMGEgpNDVG------LSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 150 dsapvvSLLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVE 229
Cdd:cd19091 135 ------PLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 230 LLAYSCLGFGTLTGKYLNGAK-PAGARNTLFSR-FTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLL 307
Cdd:cd19091 209 LLVWSPLAGGLLSGKYRRGQPaPEGSRLRRTGFdFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVII 288
|
330 340 350
....*....|....*....|....*....|
gi 2551249852 308 GATTMEQLKTNVESLHLELSEEVLAEIEAV 337
Cdd:cd19091 289 GARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-337 |
1.82e-78 |
|
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: 241.83 E-value: 1.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMTFG---EQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetQGLTETYVGNWLAK-HGSREKLIVASKVSGP 91
Cdd:pfam00248 1 IGLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYG-------DGKSEELLGEALKDyPVKRDKVVIATKVPDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 92 SRNNDSGIRpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLDTLDALAEFQRAG 171
Cdd:pfam00248 74 DGPWPSGGS------KENIRKSLEESLKRLGTDYIDLYYLHWPD-----------------PDTPIEETWDALEELKKEG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 172 KIRYIGVSNETAfgvmRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYLNGAKP 251
Cdd:pfam00248 131 KIRAIGVSNFDA----EQIEKALTKGKIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 252 agaRNTLFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHLELSEEVL 331
Cdd:pfam00248 207 ---GPGERRRLLKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEV 283
|
....*.
gi 2551249852 332 AEIEAV 337
Cdd:pfam00248 284 ARIDEL 289
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-335 |
5.76e-78 |
|
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: 241.33 E-value: 5.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 2 QYHRIPHSSLEVSTLGLGTMTFGEQNS------EADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAK 75
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWrpwvldEEESRPIIKRALDLGINFFDTANVY-------SGGASEEILGRALKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 76 HGSREKLIVASKVSGPSRN--NDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWpqrptncfgklgysWTDSAP 153
Cdd:cd19079 74 FAPRDEVVIATKVYFPMGDgpNGRG------LSRKHIMAEVDASLKRLGTDYIDLYQIHR--------------WDYETP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 154 VvslLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAY 233
Cdd:cd19079 134 I---EETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPW 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 234 SCLGFGTLTGKYLNGAKPAGARNTLFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTME 313
Cdd:cd19079 211 SPLARGRLARPWGDTTERRRSTTDTAKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLE 290
|
330 340
....*....|....*....|..
gi 2551249852 314 QLKTNVESLHLELSEEVLAEIE 335
Cdd:cd19079 291 HLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-320 |
2.46e-77 |
|
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: 237.03 E-value: 2.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 14 STLGLGTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHGSREKLIVASKVSGPSR 93
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVY-------GDGRSERLLGRWLKGRGNRDDVVIATKGGHPPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 94 NNDSGIRpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLDTLDALAEFQRAGKI 173
Cdd:cd06660 74 GDPSRSR----LSPEHIRRDLEESLRRLGTDYIDLYYLHRDD-----------------PSTPVEETLEALNELVREGKI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 174 RYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSF-EVGLAEVSQYEGVELLAYSCLGFGtltgkylngakpa 252
Cdd:cd06660 133 RYIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249852 253 garntlfsrftrysgeqtqkavaayvdiakrhnldPAQMALAFVRRQPFVASTLLGATTMEQLKTNVE 320
Cdd:cd06660 200 -----------------------------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-337 |
9.26e-77 |
|
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: 237.48 E-value: 9.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 13 VSTLGLGTMTFG---------EQNSEADAHAQLDyavvQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHgsREKLI 83
Cdd:cd19085 1 VSRLGLGCWQFGggywwgdqdDEESIATIHAALD----AGINFFDTAEAY-------GDGHSEEVLGKALKGR--RDDVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 84 VASKVSGpsrnndsgirpnQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPtncfgklgyswtdsapvVSLLDTLDA 163
Cdd:cd19085 68 IATKVSP------------DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSD-----------------VPLEETMEA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 164 LAEFQRAGKIRYIGVSNetaFGVMrylHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTG 243
Cdd:cd19085 119 LEKLKEEGKIRAIGVSN---FGPA---QLEEALDAGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 244 KYLNGAK-PAG-ARNTLFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVES 321
Cdd:cd19085 193 KFSSAEDfPPGdARTRLFRHFEPGAEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAA 272
|
330
....*....|....*.
gi 2551249852 322 LHLELSEEVLAEIEAV 337
Cdd:cd19085 273 VDLELSPSVLERLDEI 288
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
9-335 |
2.30e-74 |
|
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: 232.11 E-value: 2.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 9 SSLEVSTLGLGTMTFGEQ----NSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAkhGSREKLIV 84
Cdd:cd19080 6 SGLRVSPLALGTMTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNY-------TNGTSERLLGEFIA--GNRDRIVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 85 ASKVSGPSRNNDSGIRPNQaldRKNIREALHDSLKRLQTDYLDLYQVHWpqrptncfgklgysWTDSAPVVSLLDTLDAL 164
Cdd:cd19080 77 ATKYTMNRRPGDPNAGGNH---RKNLRRSVEASLRRLQTDYIDLLYVHA--------------WDFTTPVEEVMRALDDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 165 AefqRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGK 244
Cdd:cd19080 140 V---RAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 245 YLNGAKPAGARNTLFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHL 324
Cdd:cd19080 217 YQRGEEGRAGEAKGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL 296
|
330
....*....|.
gi 2551249852 325 ELSEEVLAEIE 335
Cdd:cd19080 297 TLSPEQLARLD 307
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
11-330 |
3.16e-72 |
|
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: 226.32 E-value: 3.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGT-MTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetQGLTETYVGNWLAKHgSREKLIVASKVS 89
Cdd:cd19074 2 LKVSELSLGTwLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYA-------AGQAEEVLGKALKGW-PRESYVISTKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 90 GP--SRNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHwpqRPtncfgklgyswtDsaPVVSLLDTLDALAEF 167
Cdd:cd19074 74 WPtgPGPNDRG------LSRKHIFESIHASLKRLQLDYVDIYYCH---RY------------D--PETPLEETVRAMDDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 168 QRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYLN 247
Cdd:cd19074 131 IRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 248 GAKP---AGARNTLFSRF-TRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLH 323
Cdd:cd19074 211 GIPPpsrSRATDEDNRDKkRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASG 290
|
....*..
gi 2551249852 324 LELSEEV 330
Cdd:cd19074 291 VKLSPEV 297
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-335 |
7.52e-56 |
|
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: 182.81 E-value: 7.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 12 EVSTLGLGTMTFGEQNS-----EADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHGsREKLIVAS 86
Cdd:cd19072 3 EVPVLGLGTWGIGGGMSkdysdDKKAIEALRYAIELGINLIDTAEMY-------GGGHAEELVGKAIKGFD-REDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVSgPSRnndsgirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLDTLDALAE 166
Cdd:cd19072 75 KVS-PDH-----------LKYDDVIKAAKESLKRLGTDYIDLYLIHWPN-----------------PSIPIEETLRAMEE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNETAFGVMRYLHLADKHDlprIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYL 246
Cdd:cd19072 126 LVEEGKIRYIGVSNFSLEELEEAQSYLKKGP---IVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 247 ngakpagaRNTLfsrftrysgeqtqkavaayVDIAKRHNLDPAQMALAFVRRQPFVAsTLLGATTMEQLKTNVESLHLEL 326
Cdd:cd19072 203 --------SPLL-------------------DEIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAGALGWEL 254
|
....*....
gi 2551249852 327 SEEVLAEIE 335
Cdd:cd19072 255 SEEDLQRLD 263
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-335 |
8.05e-54 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 178.58 E-value: 8.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 12 EVSTLGLGTMTFGEQ-------NSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHGSREKLIV 84
Cdd:cd19093 1 EVSPLGLGTWQWGDRlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVY-------GTGRSERLLGRFLKELGDRDEVVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 85 ASKVSG-PSRNNdsgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtdsAPVVSLLDTL-D 162
Cdd:cd19093 74 ATKFAPlPWRLT-----------RRSVVKALKASLERLGLDSIDLYQLHWP-----------------GPWYSQIEALmD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 163 ALAEFQRAGKIRYIGVSNetaFGV--MRYLHLA-DKHDLPrIATIQNPYSLLNRSFEV-GLAEVSQYEGVELLAYSCLGF 238
Cdd:cd19093 126 GLADAVEEGLVRAVGVSN---YSAdqLRRAHKAlKERGVP-LASNQVEYSLLYRDPEQnGLLPACDELGITLIAYSPLAQ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 239 GTLTGKYLNGAKPAGARNTLFSrftRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVAstLLGATTMEQLKTN 318
Cdd:cd19093 202 GLLTGKYSPENPPPGGRRRLFG---RKNLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAKGVVP--IPGAKNAEQAEEN 276
|
330
....*....|....*..
gi 2551249852 319 VESLHLELSEEVLAEIE 335
Cdd:cd19093 277 AGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-321 |
2.28e-53 |
|
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: 175.74 E-value: 2.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMTFGEQN----SEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHgsREKLIVAS 86
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWwgdvDDAEAIRALRAALDLGINFFDTADVY-------GDGHSERLLGKALKGR--RDKVVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsGPSRNNDSGIRPNqaLDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgySWTDSapVVSLLDTLDALAE 166
Cdd:cd19086 72 KF-GNRFDGGPERPQD--FSPEYIREAVEASLKRLGTDYIDLYQLH--------------NPPDE--VLDNDELFEALEK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNETAfgvmRYLHLADKHdlPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKyl 246
Cdd:cd19086 133 LKQEGKIRAYGVSVGDP----EEALAALRR--GGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK-- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249852 247 ngakpagarntlfsrftrysgeqtqkavaayvdiakrhnldPAQMALAFVRRQPFVASTLLGATTMEQLKTNVES 321
Cdd:cd19086 205 -----------------------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-336 |
9.33e-53 |
|
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: 176.32 E-value: 9.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 13 VSTLGLGT---------MTFGEQNsEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLT--ETYVGNWLAkhGSREK 81
Cdd:cd19102 1 LTTIGLGTwaiggggwgGGWGPQD-DRDSIAAIRAALDLGINWIDTAAVY---------GLGhsEEVVGRALK--GLRDR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 82 LIVASKVSgpsRNNDSGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNcfgklgyswtdsapvvsLLDTL 161
Cdd:cd19102 69 PIVATKCG---LLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEP-----------------IEEAW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 162 DALAEFQRAGKIRYIGVSNetaFGVMRYLHLADKHDlprIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTL 241
Cdd:cd19102 129 GALAELKEEGKVRAIGVSN---FSVDQMKRCQAIHP---IASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 242 TGK----YLNGAKPAGARNtlFSRFtrYSGE---QTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQ 314
Cdd:cd19102 203 TGKmtpeRVASLPADDWRR--RSPF--FQEPnlaRNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQ 278
|
330 340
....*....|....*....|..
gi 2551249852 315 LKTNVESLHLELSEEVLAEIEA 336
Cdd:cd19102 279 IDETVGAADLRLTPEELAEIEA 300
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-336 |
7.45e-51 |
|
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: 171.69 E-value: 7.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 3 YHRIPHSSLEVSTLGLGT------MTFGEQNsEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNwlAKH 76
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTwaigggPWWGGSD-DNESIRTIHAALDLGINLIDTAPAY-------GFGHSEEIVGK--AIK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 77 GSREKLIVASKVS-------GPSRNNDSGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswt 149
Cdd:cd19149 71 GRRDKVVLATKCGlrwdregGSFFFVRDGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVET----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 150 dsaPVVsllDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADkhdlprIATIQNPYSLLNRSFEVGLAEVSQYEGVE 229
Cdd:cd19149 140 ---PIE---ETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQ------LDIIQEKYSMLDRGIEKELLPYCKKNNIA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 230 LLAYSCLGFGTLTGK----YLNGAKPAGARNTLFSRFTRysgEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVAST 305
Cdd:cd19149 208 FQAYSPLEQGLLTGKitpdREFDAGDARSGIPWFSPENR---EKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSA 284
|
330 340 350
....*....|....*....|....*....|.
gi 2551249852 306 LLGATTMEQLKTNVESLHLELSEEVLAEIEA 336
Cdd:cd19149 285 LCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
9-334 |
5.06e-50 |
|
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: 168.93 E-value: 5.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 9 SSLEVSTLGLGTM---TFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHgsREKLIVA 85
Cdd:cd19076 8 QGLEVSALGLGCMgmsAFYGPADEEESIATLHRALELGVTFLDTADMY-------GPGTNEELLGKALKDR--RDEVVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 86 SKVsGPSRNNDSGIRPNQAlDRKNIREALHDSLKRLQTDYLDLYQVHwpqRPTncfgklgyswtdsaPVVSLLDTLDALA 165
Cdd:cd19076 79 TKF-GIVRDPGSGFRGVDG-RPEYVRAACEASLKRLGTDVIDLYYQH---RVD--------------PNVPIEETVGAMA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 166 EFQRAGKIRYIGVSNETAFGVMRylhladKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKY 245
Cdd:cd19076 140 ELVEEGKVRYIGLSEASADTIRR------AHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 246 lngAKPAGARNTLFSRFT-RYSGE---QTQKAVAAYVDIAKRHNLDPAQMALAFVRRQ-------PfvastllGATTMEQ 314
Cdd:cd19076 214 ---KSPEDLPEDDFRRNNpRFQGEnfdKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQgddivpiP-------GTKRIKY 283
|
330 340
....*....|....*....|
gi 2551249852 315 LKTNVESLHLELSEEVLAEI 334
Cdd:cd19076 284 LEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-322 |
1.21e-49 |
|
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: 167.73 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 14 STLGLGTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPvppRPETQGLTETYVGNWLAKHGSREKLIVASKVSGPSR 93
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYG---DWVERGASERVIGEWLKSRGNRDKVVIATKGGHPDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 94 NNDSGIRpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHW--PQRptncfgklgyswtdsaPVVSLLDTLDalaEFQRAG 171
Cdd:cd19082 78 EDMSRSR----LSPEDIRADLEESLERLGTDYIDLYFLHRddPSV----------------PVGEIVDTLN---ELVRAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 172 KIRYIGVSN------ETAfgvMRYlhlADKHDLPRIATIQNPYSL--LNRSFEVGLAEVSQYE---------GVELLAYS 234
Cdd:cd19082 135 KIRAFGASNwsteriAEA---NAY---AKAHGLPGFAASSPQWSLarPNEPPWPGPTLVAMDEemrawheenQLPVFAYS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 235 CLGFGtltgkYLNGAKPAGARNTLFSRFTRYSgeQTQKAVAAYVD-IAKRHNLDPAQMALAFVRRQPFVASTLLGATTME 313
Cdd:cd19082 209 SQARG-----FFSKRAAGGAEDDSELRRVYYS--EENFERLERAKeLAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPE 281
|
....*....
gi 2551249852 314 QLKTNVESL 322
Cdd:cd19082 282 QLRDSLAAA 290
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-337 |
3.69e-49 |
|
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: 167.39 E-value: 3.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHG-S 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVY-------ANGQSEEIMGQAIKELGwP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKV----SGPSrNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHwpqRPtncfgklgyswtDsaPV 154
Cdd:cd19143 74 RSDYVVSTKIfwggGGPP-PNDRG------LSRKHIVEGTKASLKRLQLDYVDLVFCH---RP------------D--PA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 155 VSLLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRS-FEVGLAEVSQYEGVELLAY 233
Cdd:cd19143 130 TPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 234 SCLGFGTLTGKYLNGAkPAGARNTLFSRF---TRYS--GEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLG 308
Cdd:cd19143 210 SPLASGLLTGKYNNGI-PEGSRLALPGYEwlkDRKEelGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITG 288
|
330 340 350
....*....|....*....|....*....|.
gi 2551249852 309 ATTMEQLKTNVESLHL--ELSEEVLAEIEAV 337
Cdd:cd19143 289 ATKVEQLEENLKALEVlpKLTPEVMEKIEAI 319
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-332 |
2.59e-47 |
|
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: 162.04 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 3 YHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVPPrpetqGLTETYVGNWL--AKHGSR 79
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLwHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPP-----GSAEENFGRILkrDLRPYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 80 EKLIVASKV---SGPSRNNDSGirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHwpqRPTncfgklgyswtdsaPVVS 156
Cdd:cd19089 76 DELVISTKAgygMWPGPYGDGG-------SRKYLLASLDQSLKRMGLDYVDIFYHH---RYD--------------PDTP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 157 LLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPrIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCL 236
Cdd:cd19089 132 LEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELGVP-LIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 237 GFGTLTGKYLNGAKPAGARNTLFSRFT-RYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQL 315
Cdd:cd19089 211 AQGLLTDKYLNGIPPDSRRAAESKFLTeEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQL 290
|
330
....*....|....*...
gi 2551249852 316 KTNVESLH-LELSEEVLA 332
Cdd:cd19089 291 EDNVAALKnLDFSEEELA 308
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-322 |
5.04e-47 |
|
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: 160.96 E-value: 5.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 14 STLGLGTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVPPRPETQGLTETYVGNWLAKHGSREKLIVASKVSGPSR 93
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTEGGVGGESERLIGRWLKDRGNRDDVVIATKVGAGPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 94 NNDSGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgyswTDSaPVVSLLDTLDALAEFQRAGKI 173
Cdd:cd19752 81 DPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAH----------------VDD-RDTPLEETLEAFNELVKAGKV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 174 RYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLL----NRSFEVGLA------EVSQYEG-VELLAYSCLgfgtLT 242
Cdd:cd19752 144 RAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLrprpGADFGVQRIvtdellDYASSRPdLTLLAYSPL----LS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 243 GKYLNGAKPAGArntlfsrftRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESL 322
Cdd:cd19752 220 GAYTRPDRPLPE---------QYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
7-337 |
4.98e-46 |
|
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: 159.51 E-value: 4.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 7 PHSSLEVSTLGLGTMTFGEQN-------SEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHGSR 79
Cdd:cd19146 5 PTAGVRVSPLCLGAMSFGEAWksmmgecDKETAFKLLDAFYEQGGNFIDTANNY-------QGEESERWVGEWMASRGNR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 80 EKLIVASKVS-GPSRNNDSGIRPN-QALDRKNIREALHDSLKRLQTDYLDLYQVHWpqrptncfgklgysWTDSAPVVSL 157
Cdd:cd19146 78 DEMVLATKYTtGYRRGGPIKIKSNyQGNHAKSLRLSVEASLKKLQTSYIDILYVHW--------------WDYTTSIPEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 158 LDTLDALAEfqrAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLG 237
Cdd:cd19146 144 MQSLNHLVA---AGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 238 FGTLTgkylngaKPAGARNTLfsRFTRYSGEQTQKAV---AAYVDIAKRHNLDPAQMALAFV-RRQPFVAStLLGATTME 313
Cdd:cd19146 221 QGQFR-------TEEEFKRRG--RSGRKGGPQTEKERkvsEKLEKVAEEKGTAITSVALAYVmHKAPYVFP-IVGGRKVE 290
|
330 340
....*....|....*....|....
gi 2551249852 314 QLKTNVESLHLELSEEVLAEIEAV 337
Cdd:cd19146 291 HLKGNIEALGISLSDEEIQEIEDA 314
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
9-337 |
7.55e-45 |
|
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: 155.65 E-value: 7.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 9 SSLEVSTLGLGTMTFGEQN-----SEADAHAQLDYAVVQGINLIDVAEMYPVpprpetqGLTETYVGNWLaKHGSREKLI 83
Cdd:cd19083 7 SDIDVNPIGLGTNAVGGHNlypnlDEEEGKDLVREALDNGVNLLDTAFIYGL-------GRSEELVGEVL-KEYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 84 VASKvsGPSRNNDSGIRPNQalDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsapvvSLLDTLDA 163
Cdd:cd19083 79 IATK--GAHKFGGDGSVLNN--SPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGET-----------------PKAEAVGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 164 LAEFQRAGKIRYIGVSNETAfgvmRYLHLADKHDLprIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTG 243
Cdd:cd19083 138 LQELKDEGKIRAIGVSNFSL----EQLKEANKDGY--VDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 244 KYlngakpagARNTLF------SRFTRYSGEQTQ---KAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQ 314
Cdd:cd19083 212 KY--------TKDTKFpdndlrNDKPLFKGERFSenlDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQ 283
|
330 340
....*....|....*....|...
gi 2551249852 315 LKTNVESLHLELSEEVLAEIEAV 337
Cdd:cd19083 284 VIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
12-335 |
3.12e-44 |
|
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: 152.79 E-value: 3.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 12 EVSTLGLGTMTFGEQ-NSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAkhGSREKLIVASKVsg 90
Cdd:cd19138 10 KVPALGQGTWYMGEDpAKRAQEIEALRAGIDLGMTLIDTAEMY-------GDGGSEELVGEAIR--GRRDKVFLVSKV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 91 psrnndsgiRPNQAlDRKNIREALHDSLKRLQTDYLDLYQVHWPQRptncfgklgyswtdsapvVSLLDTLDALAEFQRA 170
Cdd:cd19138 79 ---------LPSNA-SRQGTVRACERSLRRLGTDYLDLYLLHWRGG------------------VPLAETVAAMEELKKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 171 GKIRYIGVSNetaFGVmrylhlADKHDLPRI------ATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGK 244
Cdd:cd19138 131 GKIRAWGVSN---FDT------DDMEELWAVpgggncAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 245 YLngakpagARNTlfsrftrysgeqtqkavaAYVDIAKRHNLDPAQMALAFVRRQPFVAStLLGATTMEQLKTNVESLHL 324
Cdd:cd19138 202 GL-------LENP------------------TLKEIAARHGATPAQVALAWVLRDGNVIA-IPKSGSPEHARENAAAADL 255
|
330
....*....|.
gi 2551249852 325 ELSEEVLAEIE 335
Cdd:cd19138 256 ELTEEDLAELD 266
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
11-335 |
4.67e-43 |
|
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: 150.85 E-value: 4.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTM----TFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprPETQgltETYVGNWLAkhGSREKLIVAS 86
Cdd:cd19078 2 LEVSAIGLGCMgmshGYGPPPDKEEMIELIRKAVELGITFFDTAEVYG----PYTN---EELVGEALK--PFRDQVVIAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsGPSRNNDSGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHwpqRPTncfgklgyswtdsaPVVSLLDTLDALAE 166
Cdd:cd19078 73 KF-GFKIDGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQH---RVD--------------PNVPIEEVAGTMKE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNETAfgvmRYLHLAdkHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYL 246
Cdd:cd19078 135 LIKEGKIRHWGLSEAGV----ETIRRA--HAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKID 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 247 NGAK--PAGARNTLfSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFV-RRQPFVAStLLGATTMEQLKTNVESLH 323
Cdd:cd19078 209 ENTKfdEGDDRASL-PRFTPEALEANQALVDLLKEFAEEKGATPAQIALAWLlAKKPWIVP-IPGTTKLSRLEENIGAAD 286
|
330
....*....|..
gi 2551249852 324 LELSEEVLAEIE 335
Cdd:cd19078 287 IELTPEELREIE 298
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-341 |
5.59e-43 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 152.28 E-value: 5.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTMTFgEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAkhGSRE 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRL-PRKDEEEAEALIRRAIDNGINYIDTARGY---------GDSEEFLGKALK--GPRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 81 KLIVASKVSGPSRnndsgirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCfgklgyswtdsAPVVSLLDT 160
Cdd:COG1453 69 KVILATKLPPWVR------------DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDL-----------EKVLKPGGA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 161 LDALAEFQRAGKIRYIGVSNETAFGVMRYlhLADKHDlprIATIQNPYSLLNRSFEVGLaevsqyEGVELLAYSCLGF-- 238
Cdd:COG1453 126 LEALEKAKAEGKIRHIGFSTHGSLEVIKE--AIDTGD---FDFVQLQYNYLDQDNQAGE------EALEAAAEKGIGVii 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 239 -GTLTGKYLngAKPagarntlfsrftrysgeqTQKAVAAYvdiakRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKT 317
Cdd:COG1453 195 mKPLKGGRL--ANP------------------PEKLVELL-----CPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDE 249
|
330 340
....*....|....*....|....*.
gi 2551249852 318 NVESLHLE--LSEEVLAEIEAVHQVY 341
Cdd:COG1453 250 NLKTADNLepLTEEELAILERLAEEL 275
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
11-337 |
1.38e-42 |
|
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: 149.76 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMTFG--------EQNSEADAHAQLDyavvQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHGSREKL 82
Cdd:cd19148 2 LPVSRIALGTWAIGgwmwggtdEKEAIETIHKALD----LGINLIDTAPVY-------GFGLSEEIVGKALKEYGKRDRV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 83 IVASKVsGPSRNNDSGIRPNQALDRknIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLDTLD 162
Cdd:cd19148 71 VIATKV-GLEWDEGGEVVRNSSPAR--IRKEVEDSLRRLQTDYIDLYQVHWPD-----------------PLVPIEETAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 163 ALAEFQRAGKIRYIGVSNetaFGV--MRYLHLAdkhdlPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGT 240
Cdd:cd19148 131 ALKELLDEGKIRAIGVSN---FSPeqMETFRKV-----APLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 241 LTGKYlngakpagARNTLFS--------------RFTRYsgeqtQKAVAAYVDIAK-RHNLDPAQMALAFVRRQPFVAST 305
Cdd:cd19148 203 LSGKM--------TKDTKFEgddlrrtdpkfqepRFSQY-----LAAVEELDKLAQeRYGKSVIHLAVRWLLDQPGVSIA 269
|
330 340 350
....*....|....*....|....*....|..
gi 2551249852 306 LLGATTMEQLKTNVESLHLELSEEVLAEIEAV 337
Cdd:cd19148 270 LWGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
12-335 |
1.17e-41 |
|
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: 147.59 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 12 EVSTLGLGTMTF----GEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAKH-GSREKLIVAS 86
Cdd:cd19144 12 SVPALGFGAMGLsafyGPPKPDEERFAVLDAAFELGCTFWDTADIY---------GDSEELIGRWFKQNpGKREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsGPSRNNDSGIRPNQAlDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgyswtDSAPVVSLLDTLDALAE 166
Cdd:cd19144 83 KF-GIEKNVETGEYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQH-----------------RVDGKTPIEKTVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNETAFGVMRylhladKHDLPRIATIQ---NPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTG 243
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETLRR------AHAVHPIAAVQieySPFSLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 244 KYlngAKPAGARNTLFSRFT-RYSGEQTQK---AVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNV 319
Cdd:cd19144 218 AI---RSPDDFEEGDFRRMApRFQAENFPKnleLVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENL 294
|
330
....*....|....*.
gi 2551249852 320 ESLHLELSEEVLAEIE 335
Cdd:cd19144 295 GALKVKLTEEEEKEIR 310
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-337 |
1.23e-40 |
|
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: 144.62 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 18 LGTMTFGEQNSEADAHAQ---LDYAVVQGINLIDVAEMYPvpprpetQGLTETYVGNWLAKHgsrEKLIVASKVSGpsrn 94
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAaelLDAFLERGHTEIDTARVYP-------DGTSEELLGELGLGE---RGFKIDTKANP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 ndsgiRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsapvvSLLDTLDALAEFQRAGKIR 174
Cdd:cd19075 71 -----GVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRST-----------------PLEETLAAIDELYKEGKFK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 175 YIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYLNGAKPAGa 254
Cdd:cd19075 129 EFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAG- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 255 rntlFSRF-----------TRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQpfvaSTL---------LGATTMEQ 314
Cdd:cd19075 208 ----GGRFdpnnalgklyrDRYWKPSYFEALEKVEEAAEKEGISLAEAALRWLYHH----SALdgekgdgviLGASSLEQ 279
|
330 340
....*....|....*....|....
gi 2551249852 315 LKTNVESL-HLELSEEVLAEIEAV 337
Cdd:cd19075 280 LEENLAALeKGPLPEEVVKAIDEA 303
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-331 |
6.06e-40 |
|
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: 141.92 E-value: 6.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 14 STLGLGTMTFG---EQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAKHGsREKLIVASKVSG 90
Cdd:cd19090 1 SALGLGTAGLGgvfGGVDDDEAVATIRAALDLGINYIDTAPAY---------GDSEERLGLALAELP-REPLVLSTKVGR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 91 -PSRNNDsgirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNcfgklgYSWTDSAPVvslldtLDALAEFQR 169
Cdd:cd19090 71 lPEDTAD--------YSADRVRRSVEESLERLGRDRIDLLMIHDPERVPW------VDILAPGGA------LEALLELKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 170 AGKIRYIGVSNETAFGVMRYLhladKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYLNGA 249
Cdd:cd19090 131 EGLIKHIGLGGGPPDLLRRAI----ETGDFDVVLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 250 KPAGarntlfsrftRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHLELSEE 329
Cdd:cd19090 207 RYTY----------RWLSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
..
gi 2551249852 330 VL 331
Cdd:cd19090 277 LW 278
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-335 |
6.40e-40 |
|
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: 142.76 E-value: 6.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMTF---GEQNSEADAHAQLDYAVVQGINLIDVAEMYPvPPRPEtqgLTETYVGNWLAKHG-SREKLIVAS 86
Cdd:cd19077 3 KLVGPIGLGLMGLtwrPNPTPDEEAFETMKAALDAGSNLWNGGEFYG-PPDPH---ANLKLLARFFRKYPeYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVSGpsrnNDSGIRPNqaLDRKNIREALHDSLKRL-QTDYLDLYQvhwPQRPTncfgklgyswtdsaPVVSLLDTLDALA 165
Cdd:cd19077 79 KGGL----DPDTLRPD--GSPEAVRKSIENILRALgGTKKIDIFE---PARVD--------------PNVPIEETIKALK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 166 EFQRAGKIRYIG---VSNETafgvmrylhLADKHDLPRIATIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLGFGTL 241
Cdd:cd19077 136 ELVKEGKIRGIGlseVSAET---------IRRAHAVHPIAAVEVEYSLFSREiEENGVLETCAELGIPIIAYSPLGRGLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 242 TGKYLNGAK-PAGARNTLFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQ------PfvastLLGATTMEQ 314
Cdd:cd19077 207 TGRIKSLADiPEGDFRRHLDRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQsgpkiiP-----IPGSTTLER 281
|
330 340
....*....|....*....|.
gi 2551249852 315 LKTNVESLHLELSEEVLAEIE 335
Cdd:cd19077 282 VEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-327 |
2.79e-39 |
|
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: 139.66 E-value: 2.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 13 VSTLGLGTMTF------GEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNwlAKHGSREKLIVAS 86
Cdd:cd19088 1 VSRLGYGAMRLtgpgiwGPPADREEAIAVLRRALELGVNFIDTADSY-------GPDVNERLIAE--ALHPYPDDVVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsGPSRNNDSGIRPNQalDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLDTLDALAE 166
Cdd:cd19088 72 KG-GLVRTGPGWWGPDG--SPEYLRQAVEASLRRLGLDRIDLYQLHRID-----------------PKVPFEEQLGALAE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNETAfgvmryLHLADKHDLPRIATIQNPYSLLNRSFEvGLAEVSQYEGVELLAYSCLGFGTLtgkyl 246
Cdd:cd19088 132 LQDEGLIRHIGLSNVTV------AQIEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDL----- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 247 ngAKPAGARNtlfsrftrysgeqtqkavaayvDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHLEL 326
Cdd:cd19088 200 --AQPGGLLA----------------------EVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRL 255
|
.
gi 2551249852 327 S 327
Cdd:cd19088 256 S 256
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-332 |
1.66e-38 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 139.08 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 2 QYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVPPrpetqGLTETYVGNWLAK--HGS 78
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWhNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPP-----GSAEENFGRILKEdlKPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKV-----SGPSrnNDSGirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaP 153
Cdd:cd19151 76 RDELIISTKAgytmwPGPY--GDWG-------SKKYLIASLDQSLKRMGLDYVDIFYHHRPD-----------------P 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 154 VVSLLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLAdkHDLPRIATIQNP-YSLLNRSFEVGLAEVSQYEGVELLA 232
Cdd:cd19151 130 ETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAIL--KDLGTPCLIHQPkYSMFNRWVEEGLLDVLEEEGIGCIA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 233 YSCLGFGTLTGKYLNGAkPAGARNTLFSRFTRysGEQTQKAVAAYV----DIAKRHNLDPAQMALAFVRRQPFVASTLLG 308
Cdd:cd19151 208 FSPLAQGLLTDRYLNGI-PEDSRAAKGSSFLK--PEQITEEKLAKVrrlnEIAQARGQKLAQMALAWVLRNKRVTSVLIG 284
|
330 340
....*....|....*....|....*
gi 2551249852 309 ATTMEQLKTNVESL-HLELSEEVLA 332
Cdd:cd19151 285 ASKPSQIEDAVGALdNREFSEEELA 309
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
16-336 |
5.47e-38 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 136.34 E-value: 5.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqgLTETYVGNWLAKHG-SREKLIVASKVsgpsrn 94
Cdd:COG0656 8 LGLGTW----QLPGEEAAAAVRTALEAGYRHIDTAAMY----------GNEEGVGEAIAASGvPREELFVTTKV------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 ndsgirPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRptncfgklgyswtdsapvVSLLDTLDALAEFQRAGKIR 174
Cdd:COG0656 68 ------WNDNHGYDDTLAAFEESLERLGLDYLDLYLIHWPGP------------------GPYVETWRALEELYEEGLIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 175 YIGVSNetaFGVMrylHLADKHDLPRI--ATIQNPYSLLNRSFEvgLAEVSQYEGVELLAYSCLGfgtltgkylngakpa 252
Cdd:COG0656 124 AIGVSN---FDPE---HLEELLAETGVkpAVNQVELHPYLQQRE--LLAFCREHGIVVEAYSPLG--------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 253 gaRNTLFsrftrysgeqTQKAVAayvDIAKRHNLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNVESLHLELSEEVLA 332
Cdd:COG0656 181 --RGKLL----------DDPVLA---EIAEKHGKTPAQVVLRWHLQRGVVV--IPKSVTPERIRENLDAFDFELSDEDMA 243
|
....
gi 2551249852 333 EIEA 336
Cdd:COG0656 244 AIDA 247
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-320 |
2.39e-37 |
|
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: 134.15 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 3 YHRIPHSSLEVSTLGLGTMTFGEqNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAKHgsREKL 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGR-LSQEEAAAIIRRALDLGINYFDTAPSY---------GDSEEKIGKALKGR--RDKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 83 IVASKVSGPsrnndsgirpnqalDRKNIREALHDSLKRLQTDYLDLYQVH------WPQRptnCFGKLGYswtdsapvvs 156
Cdd:cd19100 69 FLATKTGAR--------------DYEGAKRDLERSLKRLGTDYIDLYQLHavdteeDLDQ---VFGPGGA---------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 157 lldtLDALAEFQRAGKIRYIGVSNetafgvmrylHLADKH----DLPRIATIQ---NPYSLLNRSFEVGLAEVSQYEGVe 229
Cdd:cd19100 122 ----LEALLEAKEEGKIRFIGISG----------HSPEVLlralETGEFDVVLfpiNPAGDHIDSFREELLPLAREKGV- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 230 llaysclgfGTLtgkylnGAKPAGARntlfsrftrysgeqtqkavaayvDIAKRHNLDPAQmALAFVRRQPFVASTLLGA 309
Cdd:cd19100 187 ---------GVI------AMKVLAGG-----------------------RLLSGDPLDPEQ-ALRYALSLPPVDVVIVGM 227
|
330
....*....|.
gi 2551249852 310 TTMEQLKTNVE 320
Cdd:cd19100 228 DSPEELDENLA 238
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-337 |
2.47e-37 |
|
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: 135.80 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 24 GEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAKH----GSREKLIVASKVSgPSRNNDSgi 99
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIY---------GPAEELIGEFRKRLrrerDAADDVQIHTKWV-PDPGELT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 100 rpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWpqrptncfgklgysWTDSAPvvSLLDTLDALAEFQRAGKIRYIGVS 179
Cdd:cd19101 85 -----MTRAYVEAAIDRSLKRLGVDRLDLVQFHW--------------WDYSDP--GYLDAAKHLAELQEEGKIRHLGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 180 NetaFGVMRYLHLADKhdLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKYLNGAKPAGARN--- 256
Cdd:cd19101 144 N---FDTERLREILDA--GVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYLGVPEPTGPALetr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 257 --TLFSRFTRYSG--EQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHLELSEEVLA 332
Cdd:cd19101 219 slQKYKLMIDEWGgwDLFQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRA 298
|
....*
gi 2551249852 333 EIEAV 337
Cdd:cd19101 299 AIDAV 303
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
11-329 |
3.06e-37 |
|
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: 134.99 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMTFGEQNSEADAHAQ-LDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHGS-REKLIVASKv 88
Cdd:cd19092 4 LEVSRLVLGCMRLADWGESAEELLSlIEAALELGITTFDHADIY-------GGGKCEELFGEALALNPGlREKIEIQTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 89 sgpsrnndSGIRPNQA----------LDRKNIREALHDSLKRLQTDYLDLYQVHwpqRPtncfgklgyswtdsAPVVSLL 158
Cdd:cd19092 76 --------CGIRLGDDprpgrikhydTSKEHILASVEGSLKRLGTDYLDLLLLH---RP--------------DPLMDPE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 159 DTLDALAEFQRAGKIRYIGVSNetaFGVMRYLHLADKHDLPrIATIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLG 237
Cdd:cd19092 131 EVAEAFDELVKSGKVRYFGVSN---FTPSQIELLQSYLDQP-LVTNQIELSLLHTEaIDDGTLDYCQLLDITPMAWSPLG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 238 FGtltgkylngakpagarntlfsRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKT 317
Cdd:cd19092 207 GG---------------------RLFGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRS 265
|
330
....*....|..
gi 2551249852 318 NVESLHLELSEE 329
Cdd:cd19092 266 AVKALDIELTRE 277
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-332 |
8.62e-37 |
|
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: 134.22 E-value: 8.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTMTFGE---QNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLaKHG 77
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGvfgPVDEEEAIRTVHEALDSGINYIDTAPWY-------GQGRSETVLGKAL-KGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 78 SREKLIVASKVSgpsRnndSGIRPNQALD--RKNIREALHDSLKRLQTDYLDLYQVHWPQrptncFGklgyswtDSAPVV 155
Cdd:cd19163 73 PRDSYYLATKVG---R---YGLDPDKMFDfsAERITKSVEESLKRLGLDYIDIIQVHDIE-----FA-------PSLDQI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 156 sLLDTLDALAEFQRAGKIRYIGVSnetafGV-MRYLHLADKHDLPRIATIQ--NPYSLLNRSFEvGLAEVSQYEGVELLA 232
Cdd:cd19163 135 -LNETLPALQKLKEEGKVRFIGIT-----GYpLDVLKEVLERSPVKIDTVLsyCHYTLNDTSLL-ELLPFFKEKGVGVIN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 233 YSCLGFGTLTGKYLNGAKPAgarntlfsrftrysGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTM 312
Cdd:cd19163 208 ASPLSMGLLTERGPPDWHPA--------------SPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASP 273
|
330 340
....*....|....*....|
gi 2551249852 313 EQLKTNVESLHLELSEEVLA 332
Cdd:cd19163 274 ENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-321 |
7.27e-36 |
|
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: 130.43 E-value: 7.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 14 STLGLGTM-TFGEQN--SEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAkHGSREKLIVASKVsG 90
Cdd:cd19095 1 SVLGLGTSgIGRVWGvpSEAEAARLLNTALDLGINLIDTAPAY---------GRSEERLGRALA-GLRRDDLFIATKV-G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 91 PSRNndsGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNcfgklgyswTDsapvvsllDTLDALAEFQRA 170
Cdd:cd19095 70 THGE---GGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDEL---------TG--------EVLETLEDLKAA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 171 GKIRYIGVS--NETAFGVMRylhladkhdLPRIATIQNPYSLLNRSFEVGLAevsqyegvelLAYSClGFGTLTGKYLNG 248
Cdd:cd19095 130 GKVRYIGVSgdGEELEAAIA---------SGVFDVVQLPYNVLDREEEELLP----------LAAEA-GLGVIVNRPLAN 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249852 249 AKPAGArntlFSRFTRYSGEQTQKAVAAYVDIAkrhnlDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVES 321
Cdd:cd19095 190 GRLRRR----VRRRPLYADYARRPEFAAEIGGA-----TWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-322 |
1.67e-35 |
|
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: 129.63 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAqLDyavvQGINLIDVAEMYpvpprpeTQGLTETYVGNWLaKHGSRE 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRESPELLRRA-LD----LGINYFDTAEGY-------GNGNSEEIIGEAL-KGLRRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 81 KLIVASKVSGPSRNNDsgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklGYSWTDSAPVVSLLdt 160
Cdd:cd19105 68 KVFLATKASPRLDKKD----------KAELLKSVEESLKRLQTDYIDIYQLH------------GVDTPEERLLNEEL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 161 LDALAEFQRAGKIRYIGVSneTAFGVMRYL-HLADKHdlpRIATIQNPYSLLNRSFEVGLAevsqyegveLLAYSCLGFG 239
Cdd:cd19105 124 LEALEKLKKEGKVRFIGFS--THDNMAEVLqAAIESG---WFDVIMVAYNFLNQPAELEEA---------LAAAAEKGIG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 240 TLTGKYLNGAKPAGARNTLFsrftrysgeqtqkavaayvdiaKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNV 319
Cdd:cd19105 190 VVAMKTLAGGYLQPALLSVL----------------------KAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENL 247
|
...
gi 2551249852 320 ESL 322
Cdd:cd19105 248 AAA 250
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
7-335 |
1.68e-35 |
|
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: 131.49 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 7 PHSSLEVSTLGLGTMTFGEQNS-------EADAHAQLDYAVVQGINLIDVAEMYPvpprpETQglTETYVGNWLAKHGSR 79
Cdd:cd19147 4 KTAGIRVSPLILGAMSIGDAWSgfmgsmdKEQAFELLDAFYEAGGNFIDTANNYQ-----DEQ--SETWIGEWMKSRKNR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 80 EKLIVASKVSGPSRNNDSGiRPNQALDRKNIREALH----DSLKRLQTDYLDLYQVHWpqrptncfgklgYSWTDSAPVV 155
Cdd:cd19147 77 DQIVIATKFTTDYKAYEVG-KGKAVNYCGNHKRSLHvsvrDSLRKLQTDWIDILYVHW------------WDYTTSIEEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 156 slldtLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSC 235
Cdd:cd19147 144 -----MDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 236 LGFGTLTGKylnGAKPAGARNTLFSRFTRYSGEQTQKAVA---AYVDIAKRHNLDP-AQMALAFVRRQPFVASTLLGATT 311
Cdd:cd19147 219 LGGGKFQSK---KAVEERKKNGEGLRSFVGGTEQTPEEVKiseALEKVAEEHGTESvTAIALAYVRSKAPNVFPLVGGRK 295
|
330 340
....*....|....*....|....
gi 2551249852 312 MEQLKTNVESLHLELSEEVLAEIE 335
Cdd:cd19147 296 IEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-337 |
2.14e-34 |
|
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: 128.54 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 2 QYHRIPHSSLEVSTLGLGTMTFGE---QNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAkhGS 78
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGGlmgRTTREEQIAAVRRALDLGINFFDTAPSY-------GDGKSEENLGRALK--GL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVsgpsrnndsGIRPNQALDRKN-IREALHDSLKRLQTDYLDLYQVH---WPQRPTNCFGKLGYSWtdsapV 154
Cdd:cd19104 72 PAGPYITTKV---------RLDPDDLGDIGGqIERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVGGTLSTTD-----V 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 155 VSLLDTLDALAEFQRAGKIRYIGVsneTAFGVMRYLHLADKHDLPriATIQNPYSLLNRS-FEVGLAEVSQYE------- 226
Cdd:cd19104 138 LGLGGVADAFERLRSEGKIRFIGI---TGLGNPPAIRELLDSGKF--DAVQVYYNLLNPSaAEARPRGWSAQDyggiida 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 227 ----GVELLAYSCLGFGTLTGkylNGAKPAGARNTLFSRFTrysgEQTQKAvAAYVDIAKRHNLDPAQMALAFVRRQPFV 302
Cdd:cd19104 213 aaehGVGVMGIRVLAAGALTT---SLDRGREAPPTSDSDVA----IDFRRA-AAFRALAREWGETLAQLAHRFALSNPGV 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 2551249852 303 ASTLLGATTMEQLKTNVESLHL-ELSEEVLAEIEAV 337
Cdd:cd19104 285 STVLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
11-334 |
1.71e-33 |
|
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: 125.62 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTM----TFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprPETQgltETYVGNWLaKHGSREKLIVAS 86
Cdd:cd19145 10 LEVSAQGLGCMglsgDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYG----PNTN---EVLLGKAL-KDGPREKVQLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsGPSRNNDSGIRPNQalDRKNIREALHDSLKRLQTDYLDLYQVHwpqRptncfgklgyswTDSApvVSLLDTLDALAE 166
Cdd:cd19145 82 KF-GIHEIGGSGVEVRG--DPAYVRAACEASLKRLDVDYIDLYYQH---R------------IDTT--VPIEITMGELKK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNETAFGVMRylhladKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTGKyl 246
Cdd:cd19145 142 LVEEGKIKYIGLSEASADTIRR------AHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGK-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 247 nGAKPAGARNTLF-SRFTRYSGEQTQKAVAAYV---DIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESL 322
Cdd:cd19145 214 -AKLEELLENSDVrKSHPRFQGENLEKNKVLYErveALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGAL 292
|
330
....*....|..
gi 2551249852 323 HLELSEEVLAEI 334
Cdd:cd19145 293 SVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-322 |
6.50e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 120.32 E-value: 6.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMTFG---------EQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAKhgsREKLIVAS 86
Cdd:cd19097 3 LALGTAQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY---------GDSEKVLGKFLKR---LDKFKIIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVSGpsrnndsgIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHwpqRPTNCFGKLGYSWtdsapvvslldtlDALAE 166
Cdd:cd19097 71 KLPP--------LKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLH---NPDDLLKHGGKLV-------------EALLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVS----NEtafgvmryLHLADKHDLPRIatIQNPYSLLNRSFEV-GLAEVSQYEGVELLAYSClgfgtl 241
Cdd:cd19097 127 LKKEGLIRKIGVSvyspEE--------LEKALESFKIDI--IQLPFNILDQRFLKsGLLAKLKKKGIEIHARSV------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 242 tgkYLNG--AKPAGARNTLFSRFtrysgeqtQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNV 319
Cdd:cd19097 191 ---FLQGllLMEPDKLPAKFAPA--------KPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEII 259
|
...
gi 2551249852 320 ESL 322
Cdd:cd19097 260 AAF 262
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
2-332 |
9.73e-32 |
|
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: 121.02 E-value: 9.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 2 QYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVPPrpetqGLTETYVGNWLAK--HGS 78
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWhNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPP-----GSAEENFGRILREdfAGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVS-----GPSRNNDSgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHW--PQRPtncfgklgyswtds 151
Cdd:cd19150 76 RDELIISTKAGydmwpGPYGEWGS---------RKYLLASLDQSLKRMGLDYVDIFYSHRfdPDTP-------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 152 apvvsLLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIatIQNP-YSLLNRSFE-VGLAEVSQYEGVE 229
Cdd:cd19150 133 -----LEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELGTPLL--IHQPsYNMLNRWVEeSGLLDTLQELGVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 230 LLAYSCLGFGTLTGKYLNGAkPAGARNTLFSRFT-RYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLG 308
Cdd:cd19150 206 CIAFTPLAQGLLTDKYLNGI-PEGSRASKERSLSpKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIG 284
|
330 340
....*....|....*....|....*
gi 2551249852 309 ATTMEQLKTNVESL-HLELSEEVLA 332
Cdd:cd19150 285 ASRPEQLEENVGALdNLTFSADELA 309
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-337 |
1.75e-31 |
|
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: 120.92 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHG-S 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVY-------AAGKAEVILGSIIKKKGwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVS-GPSRNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPTNcfgklgyswtdSAPvvsL 157
Cdd:cd19159 74 RSSLVITTKLYwGGKAETERG------LSRKHIIEGLKGSLQRLQLEYVD---VVFANRPDS-----------NTP---M 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 158 LDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCL 236
Cdd:cd19159 131 EEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 237 GFGTLTGKYLNGAkPAGARNTLFS------RFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGAT 310
Cdd:cd19159 211 ACGIISGKYGNGV-PESSRASLKCyqwlkeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSS 289
|
330 340
....*....|....*....|....*....
gi 2551249852 311 TMEQLKTNVESLHL--ELSEEVLAEIEAV 337
Cdd:cd19159 290 TPEQLIENLGAIQVlpKMTSHVVNEIDNI 318
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-337 |
3.77e-31 |
|
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: 119.70 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHG-S 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVY-------AAGKAERTLGNILKSKGwR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVS-GPSRNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLyqVHWPQRPTNCfgklgyswtdsapvvSL 157
Cdd:cd19160 76 RSSYVVTTKIYwGGQAETERG------LSRKHIIEGLRGSLDRLQLEYVDI--VFANRSDPNS---------------PM 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 158 LDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCL 236
Cdd:cd19160 133 EEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEMQLPELYHKIGVGSVTWSPL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 237 GFGTLTGKYlNGAKPAGARNT------LFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGAT 310
Cdd:cd19160 213 ACGLITGKY-DGRVPDTCRAAvkgyqwLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVS 291
|
330 340
....*....|....*....|....*....
gi 2551249852 311 TMEQLKTNVESLHL--ELSEEVLAEIEAV 337
Cdd:cd19160 292 SAEQLIENLGSIQVlsQLTPQTVMEIDAL 320
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-324 |
2.75e-30 |
|
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: 117.16 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 3 YHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHG-SRE 80
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTwVTFGSQISDEVAEELVTLAYENGINLFDTAEVY-------AAGKAEIVLGKILKKKGwRRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 81 KLIVASKVS-GPSRNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLD 159
Cdd:cd19141 75 SYVITTKIFwGGKAETERG------LSRKHIIEGLKASLERLQLEYVDIVFANRPD-----------------PNTPMEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 160 TLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDL-PRIAtIQNPYSLLNR-SFEVGLAEVSQYEGVELLAYSCLG 237
Cdd:cd19141 132 IVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLiPPIV-EQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 238 FGTLTGKYLNGAkPAGARNTL--FS----RFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATT 311
Cdd:cd19141 211 CGILSGKYDDGV-PEYSRASLkgYQwlkeKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASS 289
|
330
....*....|...
gi 2551249852 312 MEQLKTNVESLHL 324
Cdd:cd19141 290 TEQLYENLQAIQV 302
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-335 |
5.03e-30 |
|
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: 114.89 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqgLTETYVGNWLAKHG-SREKLIVASKVsgpsrn 94
Cdd:cd19071 4 IGLGTY----KLKPEETAEAVLAALEAGYRHIDTAAAY----------GNEAEVGEAIRESGvPREELFITTKL------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 ndsgirPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgYSWTDSAPVVSLLDTLDALAEFQRAGKIR 174
Cdd:cd19071 64 ------WPTDHGYERVREALEESLKDLGLDYLDLYLIHWP-----------VPGKEGGSKEARLETWRALEELVDEGLVR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 175 YIGVSNetaFGVMrylHLAdkhDLPRIATI-----QNPYSLLNRSFEvgLAEVSQYEGVELLAYSCLGfgtltgkylnga 249
Cdd:cd19071 127 SIGVSN---FNVE---HLE---ELLAAARIkpavnQIELHPYLQQKE--LVEFCKEHGIVVQAYSPLG------------ 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 250 kpagarntlfsrftrySGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTllGATTMEQLKTNVESLHLELSEE 329
Cdd:cd19071 184 ----------------RGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIP--KSSNPERIKENLDVFDFELSEE 245
|
....*.
gi 2551249852 330 VLAEIE 335
Cdd:cd19071 246 DMAAID 251
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-337 |
1.61e-29 |
|
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: 115.57 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHG-S 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVY-------AAGKAEVVLGNIIKKKGwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVS-GPSRNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPTncfgklgyswtdsaPVVSL 157
Cdd:cd19158 74 RSSLVITTKIFwGGKAETERG------LSRKHIIEGLKASLERLQLEYVD---VVFANRPD--------------PNTPM 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 158 LDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCL 236
Cdd:cd19158 131 EETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 237 GFGTLTGKYLNGAKPAGARNT-----LFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATT 311
Cdd:cd19158 211 ACGIVSGKYDSGIPPYSRASLkgyqwLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASN 290
|
330 340
....*....|....*....|....*...
gi 2551249852 312 MEQLKTNVESLHL--ELSEEVLAEIEAV 337
Cdd:cd19158 291 AEQLMENIGAIQVlpKLSSSIVHEIDSI 318
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-329 |
1.99e-29 |
|
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: 113.82 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 12 EVSTLGLGTMTFG-----EQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLaKHGSREKLIVAS 86
Cdd:cd19137 3 KIPALGLGTWGIGgfltpDYSRDEEMVELLKTAIELGYTHIDTAEMY-------GGGHTEELVGKAI-KDFPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVSgpsrnndsgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSLLDTLDALAE 166
Cdd:cd19137 75 KVW------------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPN-----------------PNIPLEETLSAMAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNETafgvMRYLHLADKHDLPRIATIQNPYSLLNRSFEV-GLAEVSQYEGVELLAYSCLGFGTLTgky 245
Cdd:cd19137 126 GVRQGLIRYIGVSNFN----RRLLEEAISKSQTPIVCNQVKYNLEDRDPERdGLLEYCQKNGITVVAYSPLRRGLEK--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 246 lngakpagaRNTLFSRftrysgeqtqkavaayvdIAKRHNLDPAQMALAFVRRQPFVAsTLLGATTMEQLKTNVESLHLE 325
Cdd:cd19137 199 ---------TNRTLEE------------------IAKNYGKTIAQIALAWLIQKPNVV-AIPKAGRVEHLKENLKATEIK 250
|
....
gi 2551249852 326 LSEE 329
Cdd:cd19137 251 LSEE 254
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-335 |
3.78e-29 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 115.09 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVPPrpetqGLTETYVGNWLAKHGS- 78
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPP-----GSAEENFGRLLREDFAa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 -REKLIVASKVS-----GPSRNNDSgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsa 152
Cdd:PRK09912 88 yRDELIISTKAGydmwpGPYGSGGS---------RKYLLASLDQSLKRMGLEYVDIFYSHRVDENT-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 153 pvvSLLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIatIQNP-YSLLNRSFE-VGLAEVSQYEGVEL 230
Cdd:PRK09912 145 ---PMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLL--IHQPsYNLLNRWVDkSGLLDTLQNNGVGC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 231 LAYSCLGFGTLTGKYLNGAkPAGAR-----NTLFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVAST 305
Cdd:PRK09912 220 IAFTPLAQGLLTGKYLNGI-PQDSRmhregNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSV 298
|
330 340 350
....*....|....*....|....*....|.
gi 2551249852 306 LLGATTMEQLKTNVESL-HLELSEEVLAEIE 335
Cdd:PRK09912 299 LIGASRAEQLEENVQALnNLTFSTEELAQID 329
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-335 |
1.03e-28 |
|
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: 111.21 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVASKVsgpsrn 94
Cdd:cd19073 4 LGLGTW----QLRGDDCANAVKEALELGYRHIDTAEIYN----------NEAEVGEAIAESGvPREDLFITTKV------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 ndsgirPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtdsAPVVSLLDTLDALAEFQRAGKIR 174
Cdd:cd19073 64 ------WRDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWP-----------------NPTVPLEETLGALKELKEAGKVK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 175 YIGVSNETafgvMRYLHLADKHDLPRIATIQNPYS-LLNRSfevGLAEVSQYEGVELLAYSCLgfgtltgkylngakpag 253
Cdd:cd19073 121 SIGVSNFT----IELLEEALDISPLPIAVNQVEFHpFLYQA---ELLEYCRENDIVITAYSPL----------------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 254 ARNTLFsrftrysgeqtqkAVAAYVDIAKRHNLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNVESLHLELSEEVLAE 333
Cdd:cd19073 177 ARGEVL-------------RDPVIQEIAEKYDKTPAQVALRWLVQKGIVV--IPKASSEDHLKENLAIFDWELTSEDVAK 241
|
..
gi 2551249852 334 IE 335
Cdd:cd19073 242 ID 243
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-322 |
1.07e-28 |
|
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: 111.50 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 14 STLGLGTMTF----GEQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetQGLTETYVGNWLaKHGSREKLIVASKVS 89
Cdd:cd19096 1 SVLGFGTMRLpesdDDSIDEEKAIEMIRYAIDAGINYFDTAYGYG-------GGKSEEILGEAL-KEGPREKFYLATKLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 90 gpsrnndsgirPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYswtdsapvvsllDTLDALAEFQR 169
Cdd:cd19096 73 -----------PWSVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKARKG------------GLLEFLEKAKK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 170 AGKIRYIGVSnetaFgvmrylhladkHDLPR-----IAT-----IQNPYSLLNRSFE--VGLAEVSQYEGVELLAYSCLG 237
Cdd:cd19096 130 EGLIRHIGFS----F-----------HDSPEllkeiLDSydfdfVQLQYNYLDQENQagRPGIEYAAKKGMGVIIMEPLK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 238 FGTLtgkyLNGAKPAgarntlfsrftrysgeqtqkavaayVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKT 317
Cdd:cd19096 195 GGGL----ANNPPEA-------------------------LAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDE 245
|
....*
gi 2551249852 318 NVESL 322
Cdd:cd19096 246 NIAAA 250
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-320 |
1.19e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 112.80 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMTFGEqNSEADAHAQ--LDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAK-----HGSREKLI 83
Cdd:cd19099 1 LTLSSLGLGTYRGDS-DDETDEEYReaLKAALDSGINVIDTAINY-------RGGRSERLIGKALREliekgGIKRDEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 84 VASKVSGPSRNNDSGIRP---------------------NQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfg 142
Cdd:cd19099 73 IVTKAGYIPGDGDEPLRPlkyleeklgrglidvadsaglRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQL---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 143 klgySWTDSAPVVSLL-DTLDALAEFQRAGKIRYIGVSNETAF----GVMRYLHLADKH--------DLPRIATIQNPYS 209
Cdd:cd19099 149 ----LELGEEEFYDRLeEAFEALEEAVAEGKIRYYGISTWDGFrappALPGHLSLEKLVaaaeevggDNHHFKVIQLPLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 210 LLNRSFEVGLAEVSQyEGVELL--AYScLGFGTLTGKYLNGAKPAGarntlfsrftrysgeqtqkAVAAYVDIAKRHNLD 287
Cdd:cd19099 225 LLEPEALTEKNTVKG-EALSLLeaAKE-LGLGVIASRPLNQGQLLG-------------------ELRLADLLALPGGAT 283
|
330 340 350
....*....|....*....|....*....|...
gi 2551249852 288 PAQMALAFVRRQPFVASTLLGATTMEQLKTNVE 320
Cdd:cd19099 284 LAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-337 |
2.95e-26 |
|
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: 106.39 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 1 MQYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHG-S 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWsTFSTAISEEQAEEIVTLAYENGINYFDTSDAF-------TSGQAETELGRILKKKGwK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVSGPSRNNDSGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgKLgyswtDS-APVVSL 157
Cdd:cd19142 74 RSSYIVSTKIYWSYGSEERG------LSRKHIIESVRASLRRLQLDYIDIVIIH----------KA-----DPmCPMEEV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 158 LDTLDALAEfqrAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCL 236
Cdd:cd19142 133 VRAMSYLID---NGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREkMELYMPELYNKVGVGLITWSPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 237 GFGTLTGKYL-------NGAKPAGARNTlfSRFTRYSGEQTQKA---VAAYVDIAKRHNLDPAQMALAFVRRQPFVASTL 306
Cdd:cd19142 210 SLGLDPGISEetrrlvtKLSFKSSKYKV--GSDGNGIHEETRRAshkLRELSLIAERLGCDLTQLLIAWSLKNENVQCVL 287
|
330 340 350
....*....|....*....|....*....|...
gi 2551249852 307 LGATTMEQLKTNVESLHL--ELSEEVLAEIEAV 337
Cdd:cd19142 288 IGASSLEQLYSQLNSLQLlpKLNSAVMEELERI 320
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
2-336 |
1.74e-25 |
|
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: 102.72 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 2 QYHRIPhsslevsTLGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SRE 80
Cdd:cd19140 4 NGVRIP-------ALGLGTY----PLTGEECTRAVEHALELGYRHIDTAQMYG----------NEAQVGEAIAASGvPRD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 81 KLIVASKVsGPsrNNDSgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtdsAPVVSLLDT 160
Cdd:cd19140 63 ELFLTTKV-WP--DNYS---------PDDFLASVEESLRKLRTDYVDLLLLHWP-----------------NKDVPLAET 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 161 LDALAEFQRAGKIRYIGVSNetaFGVMRYLHLADKHDLPrIATIQ---NPY----SLLNRSFEVGLAevsqyegveLLAY 233
Cdd:cd19140 114 LGALNEAQEAGLARHIGVSN---FTVALLREAVELSEAP-LFTNQveyHPYldqrKLLDAAREHGIA---------LTAY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 234 SCLGFGTLTGKYLngakpagarntlfsrftrysgeqtqkavaaYVDIAKRHNLDPAQMALAFVRRQPFVAStLLGATTME 313
Cdd:cd19140 181 SPLARGEVLKDPV------------------------------LQEIGRKHGKTPAQVALRWLLQQEGVAA-IPKATNPE 229
|
330 340
....*....|....*....|...
gi 2551249852 314 QLKTNVESLHLELSEEVLAEIEA 336
Cdd:cd19140 230 RLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-334 |
4.59e-25 |
|
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: 102.44 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 14 STLGLGTMTFGEQN--SEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHgSREKLIVASKVS-- 89
Cdd:cd19162 1 PRLGLGAASLGNLAraGEDEAAATLDAAWDAGIRYFDTAPLY-------GLGLSERRLGAALARH-PRAEYVVSTKVGrl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 90 --GPSRNNDSGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtDSAPVVSLLDTLDALAEF 167
Cdd:cd19162 73 lePGAAGRPAGADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDP---------------DRHLLQALTDAFPALEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 168 QRAGKIRYIGVsnetafGVMRY---LHLADKHDLPRIaTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYsclgfGTLTGK 244
Cdd:cd19162 138 RAEGVVGAIGV------GVTDWaalLRAARRADVDVV-MVAGRYTLLDRRAATELLPLCAAKGVAVVAA-----GVFNSG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 245 YLNGAKPAGARntlfsRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHL 324
Cdd:cd19162 206 ILATDDPAGDR-----YDYRPATPEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRT 280
|
330
....*....|
gi 2551249852 325 ELSEEVLAEI 334
Cdd:cd19162 281 PIPAEFWAEL 290
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
17-343 |
3.18e-24 |
|
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: 99.61 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 17 GLGTMTFGEQNSEADAHA--QLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVASKVSGPSr 93
Cdd:cd19120 10 GTGTAWYKSGDDDIQRDLvdSVKLALKAGFRHIDTAEMYG----------NEKEVGEALKESGvPREDLFITTKVSPGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 94 nndsgirpnqaldrKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgysWTDSAPVVSLLDTLDALAEFQRAGKI 173
Cdd:cd19120 79 --------------KDPREALRKSLAKLGVDYVDLYLIHSP-------------FFAKEGGPTLAEAWAELEALKDAGLV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 174 RYIGVSNetaFGVMrylHLAD--KHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLgfgtltgkylngakp 251
Cdd:cd19120 132 RSIGVSN---FRIE---DLEEllDTAKIKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPL--------------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 252 agarntlfSRFTRYSGEQTQKAVAayvDIAKRHNLDPAQMALAFVRRQPFVASTllgaTTM--EQLKTNVESLHLELSEE 329
Cdd:cd19120 191 --------SPLTRDAGGPLDPVLE---KIAEKYGVTPAQVLLRWALQKGIVVVT----TSSkeERMKEYLEAFDFELTEE 255
|
330
....*....|....
gi 2551249852 330 VLAEIEAVHQVYTY 343
Cdd:cd19120 256 EVEEIDKAGKQKHF 269
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
16-329 |
1.15e-23 |
|
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: 99.22 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMTFG---EQNSEADAHAQLDYAVVQGINLIDVAEMYPVpprpetqGLTETYVGNWLAKHGsREKLIVASKVsGPS 92
Cdd:cd19152 3 LGFGTAPLGnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGA-------GLSEERLGAALRELG-REDYVISTKV-GRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 93 RNNDSGIRPNQALDRKN--------------IREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYSWTDsapvvsLL 158
Cdd:cd19152 74 LVPLQEVEPTFEPGFWNplpfdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQA------IK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 159 DTLDALAEFQRAGKIRYIGV-SNETAFgVMRYLHLADkhdlPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLG 237
Cdd:cd19152 148 GAFRALEELREEGVIKAIGLgVNDWEV-ILRILEEAD----LDWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 238 FGTLTGKylngakpagarntlfSRFTRYSGEQTQKAVAAYVD----IAKRHNLDPAQMALAFVRRQPFVASTLLGATTME 313
Cdd:cd19152 223 SGFLAGG---------------DNFDYYEYGPAPPELIARRDrieaLCEQHGVSLAAAALQFALAPPAVASVAPGASSPE 287
|
330
....*....|....*.
gi 2551249852 314 QLKTNVESLHLELSEE 329
Cdd:cd19152 288 RVEENVALLATEIPAA 303
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-337 |
1.32e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 98.56 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 19 GTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPVpprpetqGLTETYVGNWLaKHGSREKLIVASKVSgpsrnndsg 98
Cdd:cd19103 21 GDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGM-------GASEKILGEFL-KRYPREDYIISTKFT--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 99 irPNQALDRKN-IREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtdsAPVVSLLDTLDALAEfqrAGKIRYIG 177
Cdd:cd19103 84 --PQIAGQSADpVADMLEGSLARLGTDYIDIYWIHNP-----------------ADVERWTPELIPLLK---SGKVKHVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 178 VSNETAFGVMRYLHLADKHDLPrIATIQNPYSLLNRSFE-VGLAEVSQYEGVELLAYSCLGFGTLTGKYL-NGAKPAGAr 255
Cdd:cd19103 142 VSNHNLAEIKRANEILAKAGVS-LSAVQNHYSLLYRSSEeAGILDYCKENGITFFAYMVLEQGALSGKYDtKHPLPEGS- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 256 ntlfSRFTRYSG--EQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNVESLHLELSEEVLAE 333
Cdd:cd19103 220 ----GRAETYNPllPQLEELTAVMAEIGAKHGASIAQVAIAWAIAKGTTP--IIGVTKPHHVEDAARAASITLTDDEIKE 293
|
....
gi 2551249852 334 IEAV 337
Cdd:cd19103 294 LEQL 297
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
15-337 |
4.24e-23 |
|
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: 96.55 E-value: 4.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 15 TLGLGTmtFGEQNSEaDAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWL----AKHG-SREKLIVASKVS 89
Cdd:cd19136 3 ILGLGT--FRLRGEE-EVRQAVDAALKAGYRLIDTASVYR----------NEADIGKALrdllPKYGlSREDIFITSKLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 90 gPSrnnDSGirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfGKLGYSWTDSAPVVSLLDTLDALAEFQR 169
Cdd:cd19136 70 -PK---DQG--------YEKARAACLGSLERLGTDYLDLYLIHWP-------GVQGLKPSDPRNAELRRESWRALEDLYK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 170 AGKIRYIGVSNETafgvMRYLHLADKHDLPRIATIQN---PYsLLNRSfevgLAEVSQYEGVELLAYSCLGFGTLtgkyl 246
Cdd:cd19136 131 EGKLRAIGVSNYT----VRHLEELLKYCEVPPAVNQVefhPH-LVQKE----LLKFCKDHGIHLQAYSSLGSGDL----- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 247 ngakpagarntlfsrftRYSGEQTQKAvaayvdIAKRHNLDPAQMALAFVRRQPfvASTLLGATTMEQLKTNVESLHLEL 326
Cdd:cd19136 197 -----------------RLLEDPTVLA------IAKKYGRTPAQVLLRWALQQG--IGVIPKSTNPERIAENIKVFDFEL 251
|
330
....*....|.
gi 2551249852 327 SEEVLAEIEAV 337
Cdd:cd19136 252 SEEDMAELNAL 262
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-329 |
1.25e-20 |
|
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: 90.46 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 14 STLGLGTMTFGEQN---SEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHGsREKLIVASKV-- 88
Cdd:cd19161 1 SELGLGTAGLGNLYtavSNADADATLDAAWDSGIRYFDTAPMY-------GHGLAEHRLGDFLREKP-RDEFVLSTKVgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 89 -----SGPSRNNDSG------IRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgKLGYSWTDSAPVVSL 157
Cdd:cd19161 73 llkpaREGSVPDPNGfvdplpFEIVYDYSYDGIMRSFEDSLQRLGLNRIDILYVH----------DIGVYTHGDRKERHH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 158 LDTL-----DALAEFQRAGKIRYIGVS-NET--AFGVMRYLHLadkhdlpRIATIQNPYSLLNRSFEVGLAEVSQYEGVE 229
Cdd:cd19161 143 FAQLmsggfKALEELKKAGVIKAFGLGvNEVqiCLEALDEADL-------DCFLLAGRYSLLDQSAEEEFLPRCEQRGTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 230 LLAYSCLGFGTLTgkylNGAKPAGARNTlfsrftRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGA 309
Cdd:cd19161 216 LVIGGVFNSGILA----TGTKSGAKFNY------GDAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGA 285
|
330 340
....*....|....*....|
gi 2551249852 310 TTMEQLKTNVESLHLELSEE 329
Cdd:cd19161 286 RNPAQLRQNVEAFQTDIPEE 305
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-338 |
1.59e-20 |
|
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: 89.31 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 8 HSSLEVSTLGLGTMTFGEQNSEADAHAQLDYavvqGINLIDVAEMYPVpprpetqgltETYVGNWLAKHG-SREKLIVAS 86
Cdd:cd19135 8 SNGVEMPILGLGTSHSGGYSHEAVVYALKEC----GYRHIDTAKRYGC----------EELLGKAIKESGvPREDLFLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVSgpsrNNDSGIRpnqaldrkNIREALHDSLKRLQTDYLDLYQVHWPQRPtncfgklgySWTDSAPVVsLLDTLDALAE 166
Cdd:cd19135 74 KLW----PSDYGYE--------STKQAFEASLKRLGVDYLDLYLLHWPDCP---------SSGKNVKET-RAETWRALEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNetaFGVMrylHLadkHDLPRIATI-----QNPYSLLNRsfEVGLAEVSQYEGVELLAYSCLGfgtl 241
Cdd:cd19135 132 LYDEGLCRAIGVSN---FLIE---HL---EQLLEDCSVvphvnQVEFHPFQN--PVELIEYCRDNNIVFEGYCPLA---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 242 TGKYLNgakpagarntlfsrftrysgeqtQKAVaayVDIAKRHNLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNVES 321
Cdd:cd19135 197 KGKALE-----------------------EPTV---TELAKKYQKTPAQILIRWSIQNGVV--TIPKSTKEERIKENCQV 248
|
330
....*....|....*..
gi 2551249852 322 LHLELSEEVLAEIEAVH 338
Cdd:cd19135 249 FDFSLSEEDMATLDSLH 265
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-336 |
2.51e-20 |
|
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: 88.56 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMTFGEQNSEADAHAQLDYavvqGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVASKVSGPSrn 94
Cdd:cd19139 4 FGLGTFRLKDDVVIDSVRTALEL----GYRHIDTAQIYD----------NEAAVGQAIAESGvPRDELFITTKIWIDN-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 ndsgirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtdsAP--VVSLLDTLDALAEFQRAGK 172
Cdd:cd19139 68 ----------LSKDKLLPSLEESLEKLRTDYVDLTLIHWP-----------------SPndEVPVEEYIGALAEAKEQGL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 173 IRYIGVSNETAfgvmryLHLADKHDLP---RIATIQ---NPYsLLNRsfevGLAEVSQYEGVELLAYSCLGFGtltgkyl 246
Cdd:cd19139 121 TRHIGVSNFTI------ALLDEAIAVVgagAIATNQielSPY-LQNR----KLVAHCKQHGIHVTSYMTLAYG------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 247 ngakpagarntlfsrftrysgeqtqKAVAAYV--DIAKRHNLDPAQMALAFVRRQPFVASTllGATTMEQLKTNVESLHL 324
Cdd:cd19139 183 -------------------------KVLDDPVlaAIAERHGATPAQIALAWAMARGYAVIP--SSTKREHLRSNLLALDL 235
|
330
....*....|..
gi 2551249852 325 ELSEEVLAEIEA 336
Cdd:cd19139 236 TLDADDMAAIAA 247
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
16-343 |
2.64e-20 |
|
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: 89.39 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMTFGEQnseaDAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLA---KHG--SREKLIVASKVSg 90
Cdd:cd19123 15 LGLGTWKSKPG----EVGQAVKQALEAGYRHIDCAAIYG----------NEAEIGAALAevfKEGkvKREDLWITSKLW- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 91 psrnndsgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWP-------QRPTNcfGKLGYSWTDsapvVSLLDTLDA 163
Cdd:cd19123 80 -----------NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvGFPES--GEDLLSLSP----IPLEDTWRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 164 LAEFQRAGKIRYIGVSNetaFGVMRylhLADKHDLPRIATIQN-----PYslLNRSfevGLAEVSQYEGVELLAYSCLGf 238
Cdd:cd19123 143 MEELVDKGLCRHIGVSN---FSVKK---LEDLLATARIKPAVNqvelhPY--LQQP---ELLAFCRDNGIHLTAYSPLG- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 239 gtltgkylNGAKPAGarntlfsrfTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAF-VRRQpfvASTLLGATTMEQLKT 317
Cdd:cd19123 211 --------SGDRPAA---------MKAEGEPVLLEDPVINKIAEKHGASPAQVLIAWaIQRG---TVVIPKSVNPERIQQ 270
|
330 340
....*....|....*....|....*.
gi 2551249852 318 NVESLHLELSEEVLAEIEAVHQVYTY 343
Cdd:cd19123 271 NLEAAEVELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-339 |
3.01e-19 |
|
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: 86.40 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 12 EVSTLGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVG---NWLAKHG--SREKLIVAS 86
Cdd:cd19111 3 PMPVIGLGTY----QSPPEEVRAAVDYALFVGYRHIDTALSYQ----------NEKAIGealKWWLKNGklKREEVFITT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsgpsrnndsgirPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNcFGKLGYSWTDSAPVVSLLDTLDAlae 166
Cdd:cd19111 69 KL------------PPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPCGFVN-KKDKGERELASSDVTSVWRAMEA--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNETAFGVMRYLHLAdkhdLPRIATIQ---NPYsLLNRSfevgLAEVSQYEGVELLAYSCLGFGTLTG 243
Cdd:cd19111 133 LVSEGKVKSIGLSNFNPRQINKILAYA----KVKPSNLQlecHAY-LQQRE----LRKFCNKKNIVVTAYAPLGSPGRAN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 244 KYLNGAKPagarntlfsrftrySGEQTQKAVAayvdIAKRHNLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNVESLH 323
Cdd:cd19111 204 QSLWPDQP--------------DLLEDPTVLA----IAKELDKTPAQVLLRFVLQRGTG--VLPKSTNKERIEENFEVFD 263
|
330
....*....|....*.
gi 2551249852 324 LELSEEVLAEIEAVHQ 339
Cdd:cd19111 264 FELTEEHFKKLKTLDR 279
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
11-336 |
1.50e-18 |
|
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: 83.78 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMtfgEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqgLTETYVGNWLAKHG-SREKLIVASKVS 89
Cdd:cd19133 7 VEMPILGFGVF---QIPDPEECERAVLEAIKAGYRLIDTAAAY----------GNEEAVGRAIKKSGiPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 90 gPSrnnDSGirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncFGKLGYSWtdsapvvslldtlDALAEFQR 169
Cdd:cd19133 74 -IQ---DAG--------YEKAKKAFERSLKRLGLDYLDLYLIHQP------FGDVYGAW-------------RAMEELYK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 170 AGKIRYIGVSNetaFGVMRYLHLADKHDL-PRIATIQ-NPYSLlnrsfEVGLAEVSQYEGVELLAYSCLGFGtltgkyln 247
Cdd:cd19133 123 EGKIRAIGVSN---FYPDRLVDLILHNEVkPAVNQIEtHPFNQ-----QIEAVEFLKKYGVQIEAWGPFAEG-------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 248 gakpagaRNTLFSRftrysgeqtqkavAAYVDIAKRHNLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNVESLHLELS 327
Cdd:cd19133 187 -------RNNLFEN-------------PVLTEIAEKYGKSVAQVILRWLIQRGIV--VIPKSVRPERIAENFDIFDFELS 244
|
....*....
gi 2551249852 328 EEVLAEIEA 336
Cdd:cd19133 245 DEDMEAIAA 253
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
13-337 |
4.60e-17 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 80.01 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 13 VSTLGLGTM------TFGEQNSEADAHAQLDYAVVQGINLIDVAEMYPvpPRPETQGLTEtyvgnwlAKHGSREKLIVAS 86
Cdd:PRK10376 17 VNRLGYGAMqlagpgVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYG--PHVTNQLIRE-------ALHPYPDDLTIVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsGPSRNNDSGIRPnqALDRKNIREALHDSLKRLQTDYLDL------YQVHWPQRPtncfgklgyswtdsapvvSLLDT 160
Cdd:PRK10376 88 KV-GARRGEDGSWLP--AFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEG------------------SIEEP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 161 LDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADkhdlprIATIQNPYSLLNRSFEVGLAEVSQyEGVELLAYSCL-GFG 239
Cdd:PRK10376 147 LTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAE------IVCVQNHYNLAHRADDALIDALAR-DGIAYVPFFPLgGFT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 240 TLTGKYLNgakpagarntlfsrftrysgeqtqkavaayvDIAKRHNLDPAQMALAFV-RRQPFVastLL--GATTMEQLK 316
Cdd:PRK10376 220 PLQSSTLS-------------------------------DVAASLGATPMQVALAWLlQRSPNI---LLipGTSSVAHLR 265
|
330 340
....*....|....*....|.
gi 2551249852 317 TNVESLHLELSEEVLAEIEAV 337
Cdd:PRK10376 266 ENLAAAELVLSEEVLAELDGI 286
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
11-337 |
6.86e-17 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 80.21 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMTFGE---QNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHG-SREKLIVAS 86
Cdd:PLN02587 9 LKVSSVGFGASPLGSvfgPVSEEDAIASVREAFRLGINFFDTSPYY-------GGTLSEKVLGKALKALGiPREKYVVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVSgpsrnndsgiRPNQALD--RKNIREALHDSLKRLQTDYLDLYQVHWPQrptncFGKLGyswtdsaPVVSllDTLDAL 164
Cdd:PLN02587 82 KCG----------RYGEGFDfsAERVTKSVDESLARLQLDYVDILHCHDIE-----FGSLD-------QIVN--ETIPAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 165 AEFQRAGKIRYIGVSNETaFGVMRYLhladkhdLPRIA--TIQNPYSL----LNRSFEVGLAEVSQYEGVELLAYSCLGF 238
Cdd:PLN02587 138 QKLKESGKVRFIGITGLP-LAIFTYV-------LDRVPpgTVDVILSYchysLNDSSLEDLLPYLKSKGVGVISASPLAM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 239 GTLTGKYLNGAKPAgarntlfsrftrysGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTN 318
Cdd:PLN02587 210 GLLTENGPPEWHPA--------------PPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEEN 275
|
330 340
....*....|....*....|...
gi 2551249852 319 VES-LHLELS---EEVLAEIEAV 337
Cdd:PLN02587 276 VAAaTELETSgidEELLSEVEAI 298
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-337 |
7.44e-17 |
|
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: 79.02 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 8 HSSLEVSTLGLGT--MTFGEQNSEADAHAqldyaVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIV 84
Cdd:cd19126 4 NNGTRMPWLGLGVfqTPDGDETERAVQTA-----LENGYRSIDTAAIYK----------NEEGVGEAIRESGvPREELFV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 85 ASKVsgpsRNNDsgIRPNQALDrknireALHDSLKRLQTDYLDLYQVHWPQRptncfGKLGYSWtdsapvvslldtlDAL 164
Cdd:cd19126 69 TTKL----WNDD--QRARRTED------AFQESLDRLGLDYVDLYLIHWPGK-----DKFIDTW-------------KAL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 165 AEFQRAGKIRYIGVSNetaFGVMRYLHLADKHDL-PRIATIQ-NPYsLLNRSfevgLAEVSQYEGVELLAYSCLGFGTLT 242
Cdd:cd19126 119 EKLYASGKVKAIGVSN---FQEHHLEELLAHADVvPAVNQVEfHPY-LTQKE----LRGYCKSKGIVVEAWSPLGQGGLL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 243 gkylngakpagarntlfsrftrysgeqTQKAVAAyvdIAKRHNLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNVESL 322
Cdd:cd19126 191 ---------------------------SNPVLAA---IGEKYGKSAAQVVLRWDIQHGVV--TIPKSVHASRIKENADIF 238
|
330
....*....|....*
gi 2551249852 323 HLELSEEVLAEIEAV 337
Cdd:cd19126 239 DFELSEDDMTAIDAL 253
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-339 |
8.38e-17 |
|
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: 78.97 E-value: 8.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 8 HSSLEVSTLGLGTMTFGEQNSEADAhaqLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVAS 86
Cdd:cd19157 5 NNGVKMPWLGLGVFKVEEGSEVVNA---VKTALKNGYRSIDTAAIYG----------NEEGVGKGIKESGiPREELFITS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsgpsRNNDSGIRPNQAldrknireALHDSLKRLQTDYLDLYQVHWPQRptncfGKLGYSWTdsapvvslldtldALAE 166
Cdd:cd19157 72 KV----WNADQGYDSTLK--------AFEASLERLGLDYLDLYLIHWPVK-----GKYKETWK-------------ALEK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 167 FQRAGKIRYIGVSNetaFGVMrylHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLgfgtLTGKYL 246
Cdd:cd19157 122 LYKDGRVRAIGVSN---FQVH---HLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL----MQGQLL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 247 NgakpagarNTLFsrftrysgeqtqkavaayVDIAKRHNLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNVESLHLEL 326
Cdd:cd19157 192 D--------NPVL------------------KEIAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENADVFDFEL 243
|
330
....*....|...
gi 2551249852 327 SEEVLAEIEAVHQ 339
Cdd:cd19157 244 SQEDMDKIDALNE 256
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
12-341 |
2.24e-16 |
|
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: 78.31 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 12 EVSTLGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqgLTETYVGNWLAKHG-SREKLIVASKVSg 90
Cdd:cd19117 13 EIPAVGLGTW----QSKPNEVAKAVEAALKAGYRHIDTAAIY----------GNEEEVGQGIKDSGvPREEIFITTKLW- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 91 psrnNDSGIRPNQALDRknirealhdSLKRLQTDYLDLYQVHWP-----QRPTNCFGKLGYSWTDSaPVVSLLDTLDALA 165
Cdd:cd19117 78 ----CTWHRRVEEALDQ---------SLKKLGLDYVDLYLMHWPvpldpDGNDFLFKKDDGTKDHE-PDWDFIKTWELMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 166 EFQRAGKIRYIGVSNetaFGVmRYLH--LADKHDLPRIATIQNPYSLLNRSFEvgLAEVSQYEGVELLAYSCLGfgtltg 243
Cdd:cd19117 144 KLPATGKVKAIGVSN---FSI-KNLEklLASPSAKIVPAVNQIELHPLLPQPK--LVDFCKSKGIHATAYSPLG------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 244 kylNGAKPAGARNTLfsrftrysgeqtqkavaayVDIAKRHNLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNVESlh 323
Cdd:cd19117 212 ---STNAPLLKEPVI-------------------IKIAKKHGKTPAQVIISWGLQRGYSV--LPKSVTPSRIESNFKL-- 265
|
330
....*....|....*...
gi 2551249852 324 LELSEEVLAEIEAVHQVY 341
Cdd:cd19117 266 FTLSDEEFKEIDELHKEY 283
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
4-340 |
2.46e-16 |
|
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: 78.16 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 4 HRIPhsslevsTLGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPVpprpetqgltETYVGNWLAKHG-----S 78
Cdd:cd19125 9 AKIP-------AVGLGTW----QADPGVVGNAVKTAIKEGYRHIDCAAIYGN----------EKEIGKALKKLFedgvvK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVsgpsRNNDsgirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWP---QRPTNCFGKLGYSWTDsapvv 155
Cdd:cd19125 68 REDLFITSKL----WCTD--------HAPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlKKGAHMPEPEEVLPPD----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 156 sLLDTLDALAEFQRAGKIRYIGVSNetaFGVMrylHLADKHDLPRI--ATIQNPYSLLNRSFEvgLAEVSQYEGVELLAY 233
Cdd:cd19125 131 -IPSTWKAMEKLVDSGKVRAIGVSN---FSVK---KLEDLLAVARVppAVNQVECHPGWQQDK--LHEFCKSKGIHLSAY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 234 SCLGFGTLTGKYLNGAK-PagarntlfsrftrysgeqtqkavaAYVDIAKRHNLDPAQMAL--AFVRRQpfvaSTLLGAT 310
Cdd:cd19125 202 SPLGSPGTTWVKKNVLKdP------------------------IVTKVAEKLGKTPAQVALrwGLQRGT----SVLPKST 253
|
330 340 350
....*....|....*....|....*....|
gi 2551249852 311 TMEQLKTNVESLHLELSEEVLAEIEAVHQV 340
Cdd:cd19125 254 NEERIKENIDVFDWSIPEEDFAKFSSIEQQ 283
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-336 |
2.81e-16 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 77.76 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 13 VSTLGLGTMTFGEQNSEADAHAQLDYavvqGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVASKVsgp 91
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALEL----GYRAIDTAQIYD----------NEAAVGQAIAESGvPRDELFITTKI--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 92 srnndsgIRPNQALDRknIREALHDSLKRLQTDYLDLYQVHWPQrPTNcfgklgyswtdsapVVSLLDTLDALAEFQRAG 171
Cdd:PRK11172 66 -------WIDNLAKDK--LIPSLKESLQKLRTDYVDLTLIHWPS-PND--------------EVSVEEFMQALLEAKKQG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 172 KIRYIGVSN------ETAFGVMRylhlADKhdlprIATIQ---NPYsLLNRSfevgLAEVSQYEGVELLAYSCLGFGtlt 242
Cdd:PRK11172 122 LTREIGISNftialmKQAIAAVG----AEN-----IATNQielSPY-LQNRK----VVAFAKEHGIHVTSYMTLAYG--- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 243 gkylngakpagarntlfsrftrysgeqtqKAVAAYV--DIAKRHNLDPAQMALAFVRRQPFvaSTLLGATTMEQLKTNVE 320
Cdd:PRK11172 185 -----------------------------KVLKDPViaRIAAKHNATPAQVILAWAMQLGY--SVIPSSTKRENLASNLL 233
|
330
....*....|....*.
gi 2551249852 321 SLHLELSEEVLAEIEA 336
Cdd:PRK11172 234 AQDLQLDAEDMAAIAA 249
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-339 |
6.01e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 77.38 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 29 EADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAKHG-SREKLIVASK----------VSGpsrnnds 97
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSY---------GRAEEFLGSWLRSRNiAPDAVFVGSKwgytytadwqVDA------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 98 girpnqalDRKNIREALHDSLKR-------LQTDYLDLYQVHwpqrptncfgklgySWTDSAPVVSLLDTLDALAEFQRA 170
Cdd:cd19098 98 --------AVHEVKDHSLARLLKqweetrsLLGKHLDLYQIH--------------SATLESGVLEDADVLAALAELKAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 171 GKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQyEGVELLAYSCLGFGTLTgkylngak 250
Cdd:cd19098 156 GVKIGLSLSGPQQAETLRRALEIEIDGARLFDSVQATWNLLEQSAGEALEEAHE-AGMGVIVKEALANGRLT-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 251 pagARNTlfsrftrySGEQtQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNVESLHLELSEEV 330
Cdd:cd19098 227 ---DRNP--------SPEL-APLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLEL 294
|
....*....
gi 2551249852 331 LAEIEAVHQ 339
Cdd:cd19098 295 LAALADLAE 303
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-338 |
1.03e-15 |
|
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: 76.68 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 8 HSSLEVSTLGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKH-----GSREKL 82
Cdd:cd19154 7 SNGVKMPLIGLGTW----QSKGAEGITAVRTALKAGYRLIDTAFLYQ----------NEEAIGEALAELleegvVKREDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 83 IVASKVsgpsrnndsgirPNQALDRKNIREALHDSLKRLQTDYLDLYQVH--WPQRPTNCFGKLGYSWTDSAPVVSLLDT 160
Cdd:cd19154 73 FITTKL------------WTHEHAPEDVEEALRESLKKLQLEYVDLYLIHapAAFKDDEGESGTMENGMSIHDAVDVEDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 161 LDALAEFQRAGKIRYIGVSNETAFGVMRYLHLAdkhdLPRIATIQNPYSLLNRSFEvgLAEVSQYEGVELLAYSCLGfgt 240
Cdd:cd19154 141 WRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNA----RVKPHNNQVECHLYFPQKE--LVEFCKKHNISVTSYATLG--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 241 ltgkylngaKPAgarNTLFSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAF-VRRQpfvASTLLGATTMEQLKTNV 319
Cdd:cd19154 212 ---------SPG---RANFTKSTGVSPAPNLLQDPIVKAIAEKHGKTPAQVLLRYlLQRG---IAVIPKSATPSRIKENF 276
|
330
....*....|....*....
gi 2551249852 320 ESLHLELSEEVLAEIEAVH 338
Cdd:cd19154 277 NIFDFSLSEEDMATLEEIE 295
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
16-191 |
1.55e-15 |
|
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: 75.10 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVASKVsgpsRN 94
Cdd:cd19131 13 LGLGVW----QVSNDEAASAVREALEVGYRSIDTAAIYG----------NEEGVGKAIRASGvPREELFITTKL----WN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 NDSGirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFgklgyswtdsapvvslLDTLDALAEFQRAGKIR 174
Cdd:cd19131 75 SDQG--------YDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDKY----------------VETWKALIELKKEGRVK 130
|
170
....*....|....*..
gi 2551249852 175 YIGVSNETAFGVMRYLH 191
Cdd:cd19131 131 SIGVSNFTIEHLQRLID 147
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
16-337 |
3.59e-15 |
|
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: 74.75 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPvpPRPET-QGLTETYVGNWLAKhgsREKLIVASKVsgpsRN 94
Cdd:cd19118 10 IGLGTW----QAEPGEVGAAVKIALKAGYRHLDLAKVYQ--NQHEVgQALKELLKEEPGVK---REDLFITSKL----WN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 NDSgiRPnqaldrKNIREALHDSLKRLQTDYLDLYQVHWPQ--RPTNCFGKLGYSWTDSAPV-----VSLLDTLDALAEF 167
Cdd:cd19118 77 NSH--RP------EYVEPALDDTLKELGLDYLDLYLIHWPVafKPTGDLNPLTAVPTNGGEVdldlsVSLVDTWKAMVEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 168 QRAGKIRYIGVSNETAfgvmRYLH--LADKHDLPRIATIQNPYSLLNRSfevgLAEVSQYEGVELLAYSCLGfGTLTGKY 245
Cdd:cd19118 149 KKTGKVKSIGVSNFSI----DHLQaiIEETGVVPAVNQIEAHPLLLQDE----LVDYCKSKNIHITAYSPLG-NNLAGLP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 246 LNGAKPagarntlfsrftrysgeqtqkavaAYVDIAKRHNLDPAQMALAFVRRQPFvaSTLLGATTMEQLKTNVESlhLE 325
Cdd:cd19118 220 LLVQHP------------------------EVKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSRIRSNFEQ--VE 271
|
330
....*....|..
gi 2551249852 326 LSEEvlaEIEAV 337
Cdd:cd19118 272 LSDD---EFNAV 280
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
78-339 |
5.44e-15 |
|
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: 74.40 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 78 SREKLIVASKVSgpsrnndsgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWP----------QRPTNCFGKLGYS 147
Cdd:cd19113 67 KREELFLTSKLW------------NNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieeKYPPGFYCGDGDN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 148 WTDSApvVSLLDTLDALAEFQRAGKIRYIGVSNETAfgvmrylhlADKHDLPRIATIQ--------NPYSLLNRsfevgL 219
Cdd:cd19113 135 FVYED--VPILDTWKALEKLVDAGKIKSIGVSNFPG---------ALILDLLRGATIKpavlqiehHPYLQQPK-----L 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 220 AEVSQYEGVELLAYSclGFGTLTGKYLNGAKpagARNT--LFSrftrysgEQTQKAVAAyvdiakRHNLDPAQMALAFVR 297
Cdd:cd19113 199 IEYAQKAGITITAYS--SFGPQSFVELNQGR---ALNTptLFE-------HDTIKSIAA------KHNKTPAQVLLRWAT 260
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2551249852 298 RQPFvaSTLLGATTMEQLKTNVESLHLELSEEVLAEIEAVHQ 339
Cdd:cd19113 261 QRGI--AVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDI 300
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
4-336 |
5.79e-15 |
|
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: 73.46 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 4 HRIPHsslevstLGLGTMTFgeqNSEADAHAQLDyAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKL 82
Cdd:cd19132 5 TQIPA-------IGFGTYPL---KGDEGVEAVVA-ALQAGYRLLDTAFNYE----------NEGAVGEAVRRSGvPREEL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 83 IVASKVsgpsrnndsgirPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPVVSL-LDTL 161
Cdd:cd19132 64 FVTTKL------------PGRHHGYEEALRTIEESLYRLGLDYVDLYLIHWPN-----------------PSRDLyVEAW 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 162 DALAEFQRAGKIRYIGVSN-----------ETafGVmrylhladkhdLPRIATIQ-NPYslLNRsfevglAEVSQYE--- 226
Cdd:cd19132 115 QALIEAREEGLVRSIGVSNflpehldrlidET--GV-----------TPAVNQIElHPY--FPQ------AEQRAYHreh 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 227 GVELLAYSCLGfgtltgkylngakpagarntlfsrftRYSGEQTQKAVAAyvdIAKRHNLDPAQMALAFVRRQPfvASTL 306
Cdd:cd19132 174 GIVTQSWSPLG--------------------------RGSGLLDEPVIKA---IAEKHGKTPAQVVLRWHVQLG--VVPI 222
|
330 340 350
....*....|....*....|....*....|
gi 2551249852 307 LGATTMEQLKTNVESLHLELSEEVLAEIEA 336
Cdd:cd19132 223 PKSANPERQRENLAIFDFELSDEDMAAIAA 252
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
11-319 |
6.13e-15 |
|
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: 74.11 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMTFGEQ----NSEADAHAQLDYAVVQGINLIDVAEMYpvpprpeTQGLTETYVGNWLAKHGS-REKLIVA 85
Cdd:cd19153 10 GNVSPVGLGTAALGGVygdgLEQDEAVAIVAEAFAAGINHFDTSPYY-------GAESSEAVLGKALAALQVpRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 86 SKVSgpsRNNDSGIRpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklGYSWTDSAPVVSllDTLDALA 165
Cdd:cd19153 83 TKVG---RYRDSEFD----YSAERVRASVATSLERLHTTYLDVVYLH------------DIEFVDYDTLVD--EALPALR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 166 EFQRAGKIRYIGVsneTAFGVMRYLHLADKHDLPRIATIQN--PYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTLTG 243
Cdd:cd19153 142 TLKDEGVIKRIGI---AGYPLDTLTRATRRCSPGSLDAVLSycHLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249852 244 KYLNGAKPAgarntlfsrftrySGEQTQKAVAAyVDIAKRHNLDPAQMALAF-VRRQPFVASTLLGATTMEQLKTNV 319
Cdd:cd19153 219 QGPPPWHPA-------------SGELRHYAAAA-DAVCASVEASLPDLALQYsLAAHAGVGTVLLGPSSLAQLRSML 281
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
11-325 |
9.91e-14 |
|
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: 70.64 E-value: 9.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYpvppRPET---QGLTETYVGNWlakhgSREKLIVASK 87
Cdd:cd19121 10 ASIPAVGLGTW----QAKAGEVKAAVAHALKIGYRHIDGALCY----QNEDevgEGIKEAIAGGV-----KREDLFVTTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 88 VSgpSRNNDsgiRPNQALDRknirealhdSLKRLQTDYLDLYQVHWPQR----------PTNCFGKLGYSWTdsapvVSL 157
Cdd:cd19121 77 LW--STYHR---RVELCLDR---------SLKSLGLDYVDLYLVHWPVLlnpngnhdlfPTLPDGSRDLDWD-----WNH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 158 LDTLDALAEFQRAGKIRYIGVSNETafgvMRYLH--LADKHDLPRIATIQNPYSLLNRSfevgLAEVSQYEGVELLAYSC 235
Cdd:cd19121 138 VDTWKQMEKVLKTGKTKAIGVSNYS----IPYLEelLKHATVVPAVNQVENHPYLPQQE----LVDFCKEKGILIEAYSP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 236 LGfgtLTGKYLNGAKPAgarntlfsrftrysgeqtqkavaayVDIAKRHNLDPAQMALAF-VRRQpfvASTLLGATTMEQ 314
Cdd:cd19121 210 LG---STGSPLISDEPV-------------------------VEIAKKHNVGPGTVLISYqVARG---AVVLPKSVTPDR 258
|
330
....*....|.
gi 2551249852 315 LKTNVESLHLE 325
Cdd:cd19121 259 IKSNLEIIDLD 269
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
16-241 |
1.05e-13 |
|
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: 70.27 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMTFGEQNSEADAHAqldyAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVASKVSGPsrn 94
Cdd:cd19134 14 IGLGVGELSDDEAERSVSA----ALEAGYRLIDTAAAYG----------NEAAVGRAIAASGiPRGELFVTTKLATP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 nDSGIRPNQaldrknirEALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtdSAPVVSLLDTLDALAEFQRAGKIR 174
Cdd:cd19134 77 -DQGFTASQ--------AACRASLERLGLDYVDLYLIHWP----------------AGREGKYVDSWGGLMKLREEGLAR 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249852 175 YIGVSNETAfgvmryLHLADKHDLPRIATIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLGFGTL 241
Cdd:cd19134 132 SIGVSNFTA------EHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRL 192
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
9-338 |
1.05e-13 |
|
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: 70.39 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 9 SSLEVSTLGLGTMTFGEQNSEADAhaqLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLA---KHG--SREKLI 83
Cdd:cd19116 7 DGNEIPAIALGTWKLKDDEGVRQA---VKHAIEAGYRHIDTAYLYG----------NEAEVGEAIRekiAEGvvKREDLF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 84 VASKVSgpsrnndsgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWP---QRPTNCFGKLGYSWTDsapvVSLLDT 160
Cdd:cd19116 74 ITTKLW------------NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPvafKENNDSESNGDGSLSD----IDYLET 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 161 LDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKhdlpRIATIQ---NPySLLNRSfevgLAEVSQYEGVELLAYSCLG 237
Cdd:cd19116 138 WRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCNI----KPAVNQievHP-TLTQEK----LVAYCQSNGIVVMAYSPFG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 238 FgtltgkylngAKPAGARNTLfsrfTRYSGEqtqkavaAYVDIAKRHNLDPAQMALAF-VRRQ--PFVAStllgaTTMEQ 314
Cdd:cd19116 209 R----------LVPRGQTNPP----PRLDDP-------TLVAIAKKYGKTTAQIVLRYlIDRGvvPIPKS-----SNKKR 262
|
330 340
....*....|....*....|....
gi 2551249852 315 LKTNVESLHLELSEEVLAEIEAVH 338
Cdd:cd19116 263 IKENIDIFDFQLTPEEVAALNSFN 286
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-346 |
1.49e-13 |
|
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: 70.11 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 8 HSSLEVSTLGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPvpPRPET-QGLTETyVGNwlAKHGSREKLIVAS 86
Cdd:cd19106 2 HTGQKMPLIGLGTW----KSKPGQVKAAVKYALDAGYRHIDCAAVYG--NEQEVgEALKEK-VGP--GKAVPREDLFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVSgpsrnndsgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWP---QR-----PTNCFGKLGYSWTDsapvvsLL 158
Cdd:cd19106 73 KLW------------NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPyafERgdnpfPKNPDGTIRYDSTH------YK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 159 DTLDALAEFQRAGKIRYIGVSNETAFGVmrylhladkHDLPRIATIQ--------NPYSLLNRsfevgLAEVSQYEGVEL 230
Cdd:cd19106 135 ETWKAMEKLVDKGLVKAIGLSNFNSRQI---------DDILSVARIKpavlqvecHPYLAQNE-----LIAHCKARGLVV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 231 LAYSCLGfgtltgkylngaKPagarntlfSRFTRYSGEQTQKAVAAYVDIAKRHNLDPAQMALAFVRRQPFVasTLLGAT 310
Cdd:cd19106 201 TAYSPLG------------SP--------DRPWAKPDEPVLLEEPKVKALAKKYNKSPAQILLRWQVQRGVV--VIPKSV 258
|
330 340 350
....*....|....*....|....*....|....*.
gi 2551249852 311 TMEQLKTNVESLHLELSEEVLAEIEAVHQVYTYPAP 346
Cdd:cd19106 259 TPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVP 294
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
66-346 |
2.67e-13 |
|
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: 69.44 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 66 ETYVGNWLA---KHG--SREKLIVASKVsgpsRNNDSGIrpnqaldrknIREALHDSLKRLQTDYLDLYQVHWPQrPT-- 138
Cdd:cd19112 50 EKEVGEALAeafKTGlvKREDLFITTKL----WNSDHGH----------VIEACKDSLKKLQLDYLDLYLVHFPV-ATkh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 139 NCFGKLGYSWTDSAPV-----VSLLDTLDALAEFQRAGKIRYIGVSNETAFgVMRYLhLADKHDLPRIATIQ-NPYslLN 212
Cdd:cd19112 115 TGVGTTGSALGEDGVLdidvtISLETTWHAMEKLVSAGLVRSIGISNYDIF-LTRDC-LAYSKIKPAVNQIEtHPY--FQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 213 RSfevGLAEVSQYEGVELLAYSCLGfgtltgkylngakpAGARNTlfSRFTRYSGEQTqkavAAYVDIAKRHNLDPAQMA 292
Cdd:cd19112 191 RD---SLVKFCQKHGISVTAHTPLG--------------GAAANA--EWFGSVSPLDD----PVLKDLAKKYGKSAAQIV 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249852 293 LAF-VRRQPFVastLLGATTMEQLKTNVESLHLELSEEVLAEIEAVHQVYTYPAP 346
Cdd:cd19112 248 LRWgIQRNTAV---IPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQP 299
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
16-180 |
2.21e-12 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 66.25 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMTFGEQNSEADAHAQLDYavvqGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVASKVSgpsrn 94
Cdd:PRK11565 18 LGLGVWQASNEEVITAIHKALEV----GYRSIDTAAIYK----------NEEGVGKALKEASvAREELFITTKLW----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 NDsgirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFgklgyswtdsapvvslLDTLDALAEFQRAGKIR 174
Cdd:PRK11565 79 ND---------DHKRPREALEESLKKLQLDYVDLYLMHWPVPAIDHY----------------VEAWKGMIELQKEGLIK 133
|
....*.
gi 2551249852 175 YIGVSN 180
Cdd:PRK11565 134 SIGVCN 139
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
17-340 |
3.84e-12 |
|
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: 66.11 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 17 GLGTMTFGEQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqgLTETYVG----NWLAKHGS--REKLIVASKVSg 90
Cdd:cd19122 11 AVGFGTFANEGAKGETYAAVTKALDVGYRHLDCAWFY----------LNEDEVGdavrDFLKENPSvkREDLFICTKVW- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 91 psrnndsgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWP---QRPTNCFGKLGyswtDSAPVVSLLD-------T 160
Cdd:cd19122 80 -----------NHLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPiaaEKNDQRSPKLG----PDGKYVILKDltenpepT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 161 LDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKhdLPRIATIQ-NPYsLLNRsfevglaevsqyegvELLAYsCLGFG 239
Cdd:cd19122 145 WRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKV--KPHVNQIEiHPF-LPNE---------------ELVDY-CFSND 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 240 TLTGKYlngaKPAGARNTLFSRFTRYSGEQTQKAvaayvdIAKRHNLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNV 319
Cdd:cd19122 206 ILPEAY----SPLGSQNQVPSTGERVSENPTLNE------VAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNF 273
|
330 340
....*....|....*....|.
gi 2551249852 320 ESlhLELSEEvlaEIEAVHQV 340
Cdd:cd19122 274 KS--IELSDE---DFEAINQV 289
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
16-339 |
5.68e-12 |
|
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: 65.37 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMTFGEQNSEADAhaqldyAVVQGINL----IDVAEMYPvpprpetqglTETYVGNWLAKH------GSREKLIVA 85
Cdd:cd19124 8 IGMGTASDPPSPEDIKA------AVLEAIEVgyrhFDTAAAYG----------TEEALGEALAEAlrlglvKSRDELFVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 86 SKVsgpsRNNDsgirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPtncfgKLGYSWTDSAPVVSL-LD---TL 161
Cdd:cd19124 72 SKL----WCSD--------AHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSL-----KPGKFSFPIEEEDFLpFDikgVW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 162 DALAEFQRAGKIRYIGVSNetaFGVMRYlhladkHDLPRIATIqnPYSL----LNRSFEVG-LAEVSQYEGVELLAYSCL 236
Cdd:cd19124 135 EAMEECQRLGLTKAIGVSN---FSCKKL------QELLSFATI--PPAVnqveMNPAWQQKkLREFCKANGIHVTAYSPL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 237 GfgtltgkylNGAKPAGARNTLFSrftrysgeqtqkavAAYVDIAKRHNLDPAQMALAFVRRQPfvASTLLGATTMEQLK 316
Cdd:cd19124 204 G---------APGTKWGSNAVMES--------------DVLKEIAAAKGKTVAQVSLRWVYEQG--VSLVVKSFNKERMK 258
|
330 340
....*....|....*....|...
gi 2551249852 317 TNVESLHLELSEEVLAEIEAVHQ 339
Cdd:cd19124 259 QNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
4-324 |
1.79e-11 |
|
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: 63.84 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 4 HRIPHSSLEVSTLGLGTMTFGEQ----NSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqGLTETYVGNWLAKHGS- 78
Cdd:cd19164 4 KPVALSLAGLPPLIFGAATFSYQyttdPESIPPVDIVRRALELGIRAFDTSPYY---------GPSEIILGRALKALRDe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 --REKLIVASKVS--GPSRNNDSgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgyswtdSAPV 154
Cdd:cd19164 75 fpRDTYFIITKVGryGPDDFDYS---------PEWIRASVERSLRRLHTDYLDLVYLH------------------DVEF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 155 VSLLDTLDALAEFQR---AGKIRYIGVSN--------------ETAFG----VMRYLHLadkhdlpriaTIQNpYSLLNR 213
Cdd:cd19164 128 VADEEVLEALKELFKlkdEGKIRNVGISGyplpvllrlaelarTTAGRpldaVLSYCHY----------TLQN-TTLLAY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 214 sfevgLAEVSQYEGVE-LLAYSCLGFGTLTgkylngakPAGARNtlfsrfTRYSGEQTQKAVAAYVDIAKRHNLDPAQMA 292
Cdd:cd19164 197 -----IPKFLAAAGVKvVLNASPLSMGLLR--------SQGPPE------WHPASPELRAAAAKAAEYCQAKGTDLADVA 257
|
330 340 350
....*....|....*....|....*....|...
gi 2551249852 293 LAFV-RRQPFVASTLLGATTMEQLKTNVESLHL 324
Cdd:cd19164 258 LRYAlREWGGEGPTVVGCSNVDELEEAVEAYWS 290
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
16-337 |
4.70e-11 |
|
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: 62.24 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVASKVSgpsrn 94
Cdd:cd19130 13 LGYGVF----KVPPADTQRAVATALEVGYRHIDTAAIYG----------NEEGVGAAIAASGiPRDELFVTTKLW----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 95 NDsgirpNQALDRknIREALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtdsAPVVSL-LDTLDALAEFQRAGKI 173
Cdd:cd19130 74 ND-----RHDGDE--PAAAFAESLAKLGLDQVDLYLVHWP-----------------TPAAGNyVHTWEAMIELRAAGRT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 174 RYIGVSNEtafgVMRYLHLADKHD--LPRIATIQNPYSLLNRSfevgLAEVSQYEGVELLAYSCLGFGTLTgkylnGAKP 251
Cdd:cd19130 130 RSIGVSNF----LPPHLERIVAATgvVPAVNQIELHPAYQQRT----IRDWAQAHDVKIEAWSPLGQGKLL-----GDPP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 252 AGArntlfsrftrysgeqtqkavaayvdIAKRHNLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNVESLHLELSEEVL 331
Cdd:cd19130 197 VGA-------------------------IAAAHGKTPAQIVLRWHLQKGHV--VFPKSVRRERMEDNLDVFDFDLTDTEI 249
|
....*.
gi 2551249852 332 AEIEAV 337
Cdd:cd19130 250 AAIDAL 255
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
16-339 |
4.85e-11 |
|
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: 62.93 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 16 LGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYpvpprpetqgLTETYVGNWLAK-----HGSREKLIVASKVsg 90
Cdd:cd19155 15 VGLGTW----QSSPEEIETAVDTALEAGYRHIDTAYVY----------RNEAAIGNVLKKwidsgKVKREELFIVTKL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 91 PSRNNDsgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPQrpTNCFGKLGYSWTDSAPVV------SLLDTLDAL 164
Cdd:cd19155 79 PPGGNR----------REKVEKFLLKSLEKLQLDYVDLYLIHFPV--GSLSKEDDSGKLDPTGEHkqdyttDLLDIWKAM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 165 AEFQRAGKIRYIGVSNETAFGVMRYLHLAdkhdlpRI--ATIQ---NPYsLLNRSfevgLAEVSQYEGVELLAYSCLGFG 239
Cdd:cd19155 147 EAQVDQGLTRSIGLSNFNREQMARILKNA------RIkpANLQvelHVY-LQQKD----LVDFCSTHSITVTAYAPLGSP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 240 TLTGKYLNGAKPAGARNTLFsrftrysgeqTQKAVAAyvdIAKRHNLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNV 319
Cdd:cd19155 216 GAAHFSPGTGSPSGSSPDLL----------QDPVVKA---IAERHGKSPAQVLLRWLMQRGVVV--IPKSTNAARIKENF 280
|
330 340
....*....|....*....|
gi 2551249852 320 ESLHLELSEEVLAEIEAVHQ 339
Cdd:cd19155 281 QVFDFELTEADMAKLSSLDK 300
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
110-334 |
8.93e-11 |
|
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: 61.90 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 110 IREALHDSLKRLQTDYLDLYQVHWP--------QRPTNCFGKLGYSWTDsapvvsLLDTLDALAEFQRAGKIRYIGVSNe 181
Cdd:cd19110 80 VKTACTRSLKALKLNYLDLYLIHWPmgfkpgepDLPLDRSGMVIPSDTD------FLDTWEAMEDLVIEGLVKNIGVSN- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 182 taFGVMRYLHLADKHDLpRIATIQN-----PYslLNRSfevGLAEVSQYEGVELLAYSCLGfGTLTGKYLngakpagARN 256
Cdd:cd19110 153 --FNHEQLERLLNKPGL-RVKPVTNqiechPY--LTQK---KLISFCQSRNVSVTAYRPLG-GSCEGVDL-------IDD 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249852 257 TLFSRftrysgeqtqkavaayvdIAKRHNLDPAQMALAF-VRRQPFVastLLGATTMEQLKTNVESLHLELSEEVLAEI 334
Cdd:cd19110 217 PVIQR------------------IAKKHGKSPAQILIRFqIQRNVIV---IPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
110-339 |
1.19e-10 |
|
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: 61.74 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 110 IREALHDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSWTDsapvvsLLDTLDALAEFQRAGKIRYIGVSNe 181
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPMAfkpgdeiyPRDENGKWLYHKTN------LCATWEALEACKDAGLVKSIGVSN- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 182 taFGVMRYLHLADKHDL---PRIATIQ-NPYslLNRSfevGLAEVSQYEGVELLAYSCLGfGTLTGKYLNGAKPAGARNT 257
Cdd:cd19109 157 --FNRRQLELILNKPGLkhkPVSNQVEcHPY--FTQP---KLLEFCQQHDIVIVAYSPLG-TCRDPIWVNVSSPPLLEDP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 258 LFsrftrysgeqtqkavaayVDIAKRHNLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNVESLHLELSEEVLAEIEAV 337
Cdd:cd19109 229 LL------------------NSIGKKYNKTAAQVVLRFNIQRGVVV--IPKSFNPERIKENFQIFDFSLTEEEMKDIEAL 288
|
..
gi 2551249852 338 HQ 339
Cdd:cd19109 289 NK 290
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
79-334 |
4.86e-10 |
|
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: 59.74 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVSgpsrnndsgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQ--RPtncfGKLGYSWTDSAPVV- 155
Cdd:cd19107 61 REDLFIVSKLW------------CTFHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTgfKP----GKELFPLDESGNVIp 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 156 ---SLLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLADKHDLPRIATIQ-NPYslLNRSfevGLAEVSQYEGVELL 231
Cdd:cd19107 125 sdtTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIERILNKPGLKYKPAVNQIEcHPY--LTQE---KLIQYCQSKGIVVT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 232 AYSCLGfgtltGKYLNGAKPagarntlfsrftrysGEQTQKAVAAYVDIAKRHNLDPAQMALAF-VRRQPFVASTllgAT 310
Cdd:cd19107 200 AYSPLG-----SPDRPWAKP---------------EDPSLLEDPKIKEIAAKHNKTTAQVLIRFpIQRNLVVIPK---SV 256
|
250 260
....*....|....*....|....
gi 2551249852 311 TMEQLKTNVESLHLELSEEVLAEI 334
Cdd:cd19107 257 TPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-334 |
5.26e-10 |
|
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: 59.78 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 8 HSSLEVSTLGLGTMTfgeqNSEADAHAQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWL-----AKHGSREKL 82
Cdd:cd19129 1 NGSGAIPALGFGTLI----PDPSATRNAVKAALEAGFRHFDCAERYR----------NEAEVGEAMqevfkAGKIRREDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 83 IVASKVsgpsRNNDSgiRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWP--------QRPTNCFGKLGYswtDSApv 154
Cdd:cd19129 67 FVTTKL----WNTNH--RPER------VKPAFEASLKRLQLDYLDLYLIHTPfafqpgdeQDPRDANGNVIY---DDG-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 155 VSLLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLAdkhdlpRI--ATIQ---NPYSLlnrsfEVGLAEVSQYEGVE 229
Cdd:cd19129 130 VTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAA------RIkpAVVQvesHPYLP-----EWELLDFCKNHGIV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 230 LLAYSCLGFGtLTGKYLngAKPagarntlfsrftrysgeqtqkavaAYVDIAKRHNLDPAQMALAF-VRRQpfvASTLLG 308
Cdd:cd19129 199 LQAFAPLGHG-MEPKLL--EDP------------------------VITAIARRVNKTPAQVLLAWaIQRG---TALLTT 248
|
330 340
....*....|....*....|....*.
gi 2551249852 309 ATTMEQLKTNVESlhLELSEEVLAEI 334
Cdd:cd19129 249 SKTPSRIRENFDI--STLPEDAMREI 272
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
108-329 |
1.60e-09 |
|
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: 57.92 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 108 KNIREALHDSLKRLQTDYLDLYQVHWPQ--RPTNCFGKLGYSWTDSAPVVSLLDTLDALAEFQRAGKIRYIGVSNETAFG 185
Cdd:cd19128 75 ENVKEQLLITLQDLQLEYLDLFLIHWPLafDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 186 VMrylhladkhDLPRIATIQnPYSllnRSFEV-------GLAEVSQYEGVELLAYSCLGfgtltGKYLNGAkpagarNTL 258
Cdd:cd19128 155 LT---------DLLNYCKIK-PFM---NQIEChpyfqndKLIKFCIENNIHVTAYRPLG-----GSYGDGN------LTF 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249852 259 fsrftrysgeQTQKAVAAyvdIAKRHNLDPAQMALAF-VRRQPFVASTLLGATTMEQLKTNVESLHLELSEE 329
Cdd:cd19128 211 ----------LNDSELKA---LATKYNTTPPQVIIAWhLQKWPKNYSVIPKSANKSRCQQNFDINDLALTKE 269
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-180 |
3.32e-09 |
|
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: 56.76 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 8 HSSLEVSTLGLGTMTFGEQNSEADAhaqLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAKHG-SREKLIVAS 86
Cdd:cd19156 4 ANGVEMPRLGLGVWRVQDGAEAENA---VKWAIEAGYRHIDTAAIYK----------NEEGVGQGIRESGvPREEVFVTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 87 KVsgpsRNNDSGIrpnqaldrKNIREALHDSLKRLQTDYLDLYQVHWPQRptncfGKlgyswtdsapvvsLLDTLDALAE 166
Cdd:cd19156 71 KL----WNSDQGY--------ESTLAAFEESLEKLGLDYVDLYLIHWPVK-----GK-------------FKDTWKAFEK 120
|
170
....*....|....
gi 2551249852 167 FQRAGKIRYIGVSN 180
Cdd:cd19156 121 LYKEKKVRAIGVSN 134
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
11-336 |
3.48e-09 |
|
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: 57.03 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 11 LEVSTLGLGTMtfgeQNSEADAHAQLDYAVVQGINLIDVAEMYpvppRPETQgltetyVGNWLAKHG-SREKLIVASKVS 89
Cdd:cd19127 7 VEMPALGLGVF----QTPPEETADAVATALADGYRLIDTAAAY----GNERE------VGEGIRRSGvDRSDIFVTTKLW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 90 GPSRNNDSGIRpnqALDRknirealhdSLKRLQTDYLDLYQVHWPQRptNCFGKLGYSWTDsapvvslLDTLdaLAEfqr 169
Cdd:cd19127 73 ISDYGYDKALR---GFDA---------SLRRLGLDYVDLYLLHWPVP--NDFDRTIQAYKA-------LEKL--LAE--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 170 aGKIRYIGVSNetaFGVMRYLHLADKHD-LPRIATIQ-NPYsLLNRSfevgLAEVSQYEGVELLAYSCLGfgtltGKYLN 247
Cdd:cd19127 127 -GRVRAIGVSN---FTPEHLERLIDATTvVPAVNQVElHPY-FSQKD----LRAFHRRLGIVTQAWSPIG-----GVMRY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 248 GAKPAGARNTLFSRFTrysgeqtqkavaaYVDIAKRHNLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNVESLHLELS 327
Cdd:cd19127 193 GASGPTGPGDVLQDPT-------------ITGLAEKYGKTPAQIVLRWHLQNGVSA--IPKSVHPERIAENIDIFDFALS 257
|
....*....
gi 2551249852 328 EEVLAEIEA 336
Cdd:cd19127 258 AEDMAAIDA 266
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|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
110-180 |
4.03e-08 |
|
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: 53.77 E-value: 4.03e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249852 110 IREALHDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSWTDsapvvsLLDTLDALAEFQRAGKIRYIGVSN 180
Cdd:cd19108 90 VRPALEKSLKKLQLDYVDLYLIHFPVAlkpgeelfPKDENGKLIFDTVD------LCATWEAMEKCKDAGLAKSIGVSN 162
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|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
107-336 |
1.64e-07 |
|
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: 52.17 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 107 RKNIREALHDSLKRLQTDYLDLYQVHWP--QRPTNCFGKLGYSWTD---------SAPVVSLLDTLDALAEfqrAGKIRY 175
Cdd:cd19114 77 KDHVREAFDRQLKDYGLDYIDLYLIHFPipAAYVDPAENYPFLWKDkelkkfpleQSPMQECWREMEKLVD---AGLVRN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 176 IGVSNetaFGVMRYLHLADKHDLpRIATIQ---NPYSLLNRsfevgLAEVSQYEGVELLAYSCLGfgtltgkylngakpa 252
Cdd:cd19114 154 IGIAN---FNVQLILDLLTYAKI-KPAVLQiehHPYLQQKR-----LIDWAKKQGIQITAYSSFG--------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 253 garNTLFSRFTRYSGEQTQKAVAAYVD-IAKRHNLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNVESLHLELSEE-- 329
Cdd:cd19114 210 ---NAVYTKVTKHLKHFTNLLEHPVVKkLADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTNLDITSYKLDEEdm 284
|
....*...
gi 2551249852 330 -VLAEIEA 336
Cdd:cd19114 285 eALYELEA 292
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|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
79-339 |
2.46e-07 |
|
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: 51.65 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVSgpsrnndsgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgKLGY---------SWT 149
Cdd:cd19115 70 REDLFIVSKLW------------NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPI-------ALKYvdpavryppGWF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 150 DSAPVV-----SLLDTLDALAEFQRAGKIRYIGVSNETAFGVMRYLHLAdkhdlpRI--ATIQ---NPYSLLNRsfevgL 219
Cdd:cd19115 131 YDGKKVefsnaPIQETWTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYA------RIrpATLQiehHPYLTQPR-----L 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 220 AEVSQYEGVELLAYSclGFGTLTGKYLNgakPAGARNT--LFSRFTrysgeqtqkavaaYVDIAKRHNLDPAQMALAFV- 296
Cdd:cd19115 200 VKYAQKEGIAVTAYS--SFGPQSFLELD---LPGAKDTppLFEHDV-------------IKSIAEKHGKTPAQVLLRWAt 261
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2551249852 297 RRQPFVASTLLGATTMEQlktNVESLHLELSEEVLAEIEAVHQ 339
Cdd:cd19115 262 QRGIAVIPKSNNPKRLAQ---NLDVTGFDLEAEEIKAISALDI 301
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|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-180 |
3.14e-07 |
|
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: 51.34 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 4 HRIPhsslevsTLGLGTMTFGEQNSEADAhaQLDYAVVQGINLIDVAEMYPvpprpetqglTETYVGNWLAK---HGS-- 78
Cdd:cd19119 10 ASIP-------ALGLGTASPHEDRAEVKE--AVEAAIKEGYRHIDTAYAYE----------TEDFVGEAIKRaidDGSik 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249852 79 REKLIVASKVsGPSRNNdsgirpnqaldrkNIREALHDSLKRLQTDYLDLYQVHWP-------------QRPTNCFGKLG 145
Cdd:cd19119 71 REELFITTKV-WPTFYD-------------EVERSLDESLKALGLDYVDLLLVHWPvcfekdsddsgkpFTPVNDDGKTR 136
|
170 180 190
....*....|....*....|....*....|....*
gi 2551249852 146 YSWTDSApvvslLDTLDALAEFQRAGKIRYIGVSN 180
Cdd:cd19119 137 YAASGDH-----ITTYKQLEKIYLDGRAKAIGVSN 166
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