|
Name |
Accession |
Description |
Interval |
E-value |
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1-355 |
6.39e-102 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 305.52 E-value: 6.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 1 MKHLVILGGGYGGMRILQRLlpSNQLPDDVQVTLIDKVPYHCFKTEYYALVAGTISETHIRIPFPEH-PRLNIQY--GTV 77
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRL--RKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELlRRAGVRFiqGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 78 TNIDLEEKAVHLDGGEAIQYDDLIIGLGCEDKYHNVPGAKEYTHSLQSIEQTRKTYEQLNSLEPNA------TVAVVGAG 151
Cdd:COG1252 79 TGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAerrrllTIVVVGGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 152 LSGVEVASELRE-----------SRSDLKIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN-IVYNH 219
Cdd:COG1252 159 PTGVELAGELAEllrkllrypgiDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADgVTLED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 220 DEPLECDAIVWTAGIQANEVVRNLPVEQDGSGRVVLTKYHNIPNNEHVYVVGDCAAL------PHAPSAQLAEGQGEQIV 293
Cdd:COG1252 239 GEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVpdpdgkPVPKTAQAAVQQAKVLA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446604727 294 QILLKRWHNEPLPDELPviKLKGVLGSLGKKHGFGLLANQPLMGRVPRLLKSGI--LWMYKYHN 355
Cdd:COG1252 319 KNIAALLRGKPLKPFRY--RDKGCLASLGRGAAVADVGGLKLSGFLAWLLKRAIhlYFLPGFRG 380
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
2-289 |
1.13e-33 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 126.28 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 2 KHLVILGGGYGGMRILQRLLPSNqlpddVQVTLIDK---VPYH-CFKTEYYALVAGTISETHIRIPFPEHPR-------L 70
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLG-----GKVTLIEDegtCPYGgCVLSKALLGAAEAPEIASLWADLYKRKEevvkklnN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 71 NIQY---GTVTNIDLEEKAVHL-----DGGEAIQYDDLIIGLGCEDKYHNVPGAKE-YTHSLQSIEQTrktyEQLNSLEP 141
Cdd:pfam07992 76 GIEVllgTEVVSIDPGAKKVVLeelvdGDGETITYDRLVIATGARPRLPPIPGVELnVGFLVRTLDSA----EALRLKLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 142 NATVAVVGAGLSGVEVASELRESRSdlKIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN---IVYN 218
Cdd:pfam07992 152 PKRVVVVGGGYIGVELAAALAKLGK--EVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDgdgVEVI 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446604727 219 HDEP--LECDAIVWTAGIQAN-EVVRNLPVEQDGSGRVVLTKYHNIpNNEHVYVVGDCAAlPHAPSAQLAEGQG 289
Cdd:pfam07992 230 LKDGteIDADLVVVAIGRRPNtELLEAAGLELDERGGIVVDEYLRT-SVPGIYAAGDCRV-GGPELAQNAVAQG 301
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
4-353 |
8.64e-30 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 118.33 E-value: 8.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 4 LVILGGGYGGMRILQRLLPSNQlpdDVQVTlidKVPYHCFKTeyyALVAGTISET--HIRIPFPEHPRLNIQ-----YGT 76
Cdd:PTZ00318 13 VVVLGTGWAGAYFVRNLDPKKY---NITVI---SPRNHMLFT---PLLPQTTTGTleFRSICEPVRPALAKLpnrylRAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 77 VTNIDLEEKAV----------HLDGGEAIQYDDLIIGLGCEDKYHNVPGAKEYTHSLQSIEQTRKTYEQL---------- 136
Cdd:PTZ00318 84 VYDVDFEEKRVkcgvvsksnnANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIvqcieraslp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 137 -NSLEPNA---TVAVVGAGLSGVEVASELRESRSDL------------KIYLFDRKDRILFPYPEKLSRYVEEWFVKHKV 200
Cdd:PTZ00318 164 tTSVEERKrllHFVVVGGGPTGVEFAAELADFFRDDvrnlnpelveecKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 201 TIIRNSNITKV-EPNIVYNHDEPLECDAIVWTAGIQANEVVRNLPVEQDGSGRVVLTKYHNIPNNEHVYVVGDCAAL--- 276
Cdd:PTZ00318 244 DIRTKTAVKEVlDKEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPIPNVFALGDCAANeer 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446604727 277 PHAPSAQLAEGQGEQIVQILLKRWHNEPLPDELpVIKLKGVLGSLGKKHGFGLLANQPLMGrvprlLKSGILWMYKY 353
Cdd:PTZ00318 324 PLPTLAQVASQQGVYLAKEFNNELKGKPMSKPF-VYRSLGSLAYLGNYSAIVQLGAFDLSG-----FKALLFWRSAY 394
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
100-274 |
2.01e-03 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 39.84 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 100 LIIGLGCEDKYHNVPGAKEYthslqSIeqtrkTYEQLNSLE--PNATVaVVGAGLSGVEVASELRESRSDLKIYLfdrKD 177
Cdd:TIGR01438 147 FLIATGERPRYPGIPGAKEL-----CI-----TSDDLFSLPycPGKTL-VVGASYVALECAGFLAGIGLDVTVMV---RS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 178 RILFPYPEKLSRYVEEWFVKHKVTIIRN---SNITKVEPNIVY---NHDEPL--ECDAIVWTAGIQANevVRNLPVEQDG 249
Cdd:TIGR01438 213 ILLRGFDQDCANKVGEHMEEHGVKFKRQfvpIKVEQIEAKVLVeftDSTNGIeeEYDTVLLAIGRDAC--TRKLNLENVG 290
|
170 180 190
....*....|....*....|....*....|...
gi 446604727 250 ------SGRVVLTKYH--NIPnneHVYVVGDCA 274
Cdd:TIGR01438 291 vkinkkTGKIPADEEEqtNVP---YIYAVGDIL 320
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1-355 |
6.39e-102 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 305.52 E-value: 6.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 1 MKHLVILGGGYGGMRILQRLlpSNQLPDDVQVTLIDKVPYHCFKTEYYALVAGTISETHIRIPFPEH-PRLNIQY--GTV 77
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRL--RKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELlRRAGVRFiqGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 78 TNIDLEEKAVHLDGGEAIQYDDLIIGLGCEDKYHNVPGAKEYTHSLQSIEQTRKTYEQLNSLEPNA------TVAVVGAG 151
Cdd:COG1252 79 TGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAerrrllTIVVVGGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 152 LSGVEVASELRE-----------SRSDLKIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN-IVYNH 219
Cdd:COG1252 159 PTGVELAGELAEllrkllrypgiDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADgVTLED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 220 DEPLECDAIVWTAGIQANEVVRNLPVEQDGSGRVVLTKYHNIPNNEHVYVVGDCAAL------PHAPSAQLAEGQGEQIV 293
Cdd:COG1252 239 GEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVpdpdgkPVPKTAQAAVQQAKVLA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446604727 294 QILLKRWHNEPLPDELPviKLKGVLGSLGKKHGFGLLANQPLMGRVPRLLKSGI--LWMYKYHN 355
Cdd:COG1252 319 KNIAALLRGKPLKPFRY--RDKGCLASLGRGAAVADVGGLKLSGFLAWLLKRAIhlYFLPGFRG 380
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
28-299 |
3.83e-43 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 151.89 E-value: 3.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 28 DDVQVTLIDKVPYHcfkteYYA------LVAGTI---SETHIRIP-FPEHPRLNIQYGT-VTNIDLEEKAVHLDGGEAIQ 96
Cdd:COG0446 4 PDAEITVIEKGPHH-----SYQpcglpyYVGGGIkdpEDLLVRTPeSFERKGIDVRTGTeVTAIDPEAKTVTLRDGETLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 97 YDDLIIGLGCEDKYHNVPGAK-EYTHSLQSIEQTRKTYEQLNSLEPNaTVAVVGAGLSGVEVASELResRSDLKIYLFDR 175
Cdd:COG0446 79 YDKLVLATGARPRPPPIPGLDlPGVFTLRTLDDADALREALKEFKGK-RAVVIGGGPIGLELAEALR--KRGLKVTLVER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 176 KDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN----IVYNHDEPLECDAIVWTAGIQAN-EVVRNLPVEQDGS 250
Cdd:COG0446 156 APRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDdkvaVTLTDGEEIPADLVVVAPGVRPNtELAKDAGLALGER 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446604727 251 GRVVLTKY--HNIPNnehVYVVGDCAALPHA--------PSAQLAEGQGEQIVQILLKR 299
Cdd:COG0446 236 GWIKVDETlqTSDPD---VYAAGDCAEVPHPvtgktvyiPLASAANKQGRVAAENILGG 291
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
2-289 |
1.13e-33 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 126.28 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 2 KHLVILGGGYGGMRILQRLLPSNqlpddVQVTLIDK---VPYH-CFKTEYYALVAGTISETHIRIPFPEHPR-------L 70
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLG-----GKVTLIEDegtCPYGgCVLSKALLGAAEAPEIASLWADLYKRKEevvkklnN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 71 NIQY---GTVTNIDLEEKAVHL-----DGGEAIQYDDLIIGLGCEDKYHNVPGAKE-YTHSLQSIEQTrktyEQLNSLEP 141
Cdd:pfam07992 76 GIEVllgTEVVSIDPGAKKVVLeelvdGDGETITYDRLVIATGARPRLPPIPGVELnVGFLVRTLDSA----EALRLKLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 142 NATVAVVGAGLSGVEVASELRESRSdlKIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN---IVYN 218
Cdd:pfam07992 152 PKRVVVVGGGYIGVELAAALAKLGK--EVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDgdgVEVI 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446604727 219 HDEP--LECDAIVWTAGIQAN-EVVRNLPVEQDGSGRVVLTKYHNIpNNEHVYVVGDCAAlPHAPSAQLAEGQG 289
Cdd:pfam07992 230 LKDGteIDADLVVVAIGRRPNtELLEAAGLELDERGGIVVDEYLRT-SVPGIYAAGDCRV-GGPELAQNAVAQG 301
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
4-353 |
8.64e-30 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 118.33 E-value: 8.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 4 LVILGGGYGGMRILQRLLPSNQlpdDVQVTlidKVPYHCFKTeyyALVAGTISET--HIRIPFPEHPRLNIQ-----YGT 76
Cdd:PTZ00318 13 VVVLGTGWAGAYFVRNLDPKKY---NITVI---SPRNHMLFT---PLLPQTTTGTleFRSICEPVRPALAKLpnrylRAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 77 VTNIDLEEKAV----------HLDGGEAIQYDDLIIGLGCEDKYHNVPGAKEYTHSLQSIEQTRKTYEQL---------- 136
Cdd:PTZ00318 84 VYDVDFEEKRVkcgvvsksnnANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIvqcieraslp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 137 -NSLEPNA---TVAVVGAGLSGVEVASELRESRSDL------------KIYLFDRKDRILFPYPEKLSRYVEEWFVKHKV 200
Cdd:PTZ00318 164 tTSVEERKrllHFVVVGGGPTGVEFAAELADFFRDDvrnlnpelveecKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 201 TIIRNSNITKV-EPNIVYNHDEPLECDAIVWTAGIQANEVVRNLPVEQDGSGRVVLTKYHNIPNNEHVYVVGDCAAL--- 276
Cdd:PTZ00318 244 DIRTKTAVKEVlDKEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPIPNVFALGDCAANeer 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446604727 277 PHAPSAQLAEGQGEQIVQILLKRWHNEPLPDELpVIKLKGVLGSLGKKHGFGLLANQPLMGrvprlLKSGILWMYKY 353
Cdd:PTZ00318 324 PLPTLAQVASQQGVYLAKEFNNELKGKPMSKPF-VYRSLGSLAYLGNYSAIVQLGAFDLSG-----FKALLFWRSAY 394
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1-326 |
1.78e-29 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 116.78 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 1 MKHLVILGGGYGGMRILQRLLpsnQLPDDVQVTLIDKVPYHCfkteYY-----ALVAGTISETHIRIP---FPEHPRLNI 72
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELR---KLDPDGEITVIGAEPHPP----YNrpplsKVLAGETDEEDLLLRpadFYEENGIDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 73 QYGT-VTNIDLEEKAVHLDGGEAIQYDDLIIGLGCEDKYHNVPGA-KEYTHSLQSIEQTRKTYEQLnslEPNATVAVVGA 150
Cdd:COG1251 74 RLGTrVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGAdLPGVFTLRTLDDADALRAAL---APGKRVVVIGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 151 GLSGVEVASELREsrSDLKIYLFDRKDRILfPY--PEKLSRYVEEWFVKHKVTIIRNSNITKVEPN-----IVYNHDEPL 223
Cdd:COG1251 151 GLIGLEAAAALRK--RGLEVTVVERAPRLL-PRqlDEEAGALLQRLLEALGVEVRLGTGVTEIEGDdrvtgVRLADGEEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 224 ECDAIVWTAGIQAN-EVVRN--LPVEQ----DGSGRVvltkyhnipNNEHVYVVGDCAALPHA-------PSAQLAEGQG 289
Cdd:COG1251 228 PADLVVVAIGVRPNtELARAagLAVDRgivvDDYLRT---------SDPDIYAAGDCAEHPGPvygrrvlELVAPAYEQA 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446604727 290 EQIVQILLKRwhNEPLPDELPVIKLK--GV-LGSLGKKHG 326
Cdd:COG1251 299 RVAAANLAGG--PAAYEGSVPSTKLKvfGVdVASAGDAEG 336
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
72-274 |
1.61e-11 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 64.37 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 72 IQYGTVTNIDLEE--KAVHLDGGEAIQYDDLIIGLGCEDKYHNVPGAKEYTH---SLQSIEQTRKTyeqlnslePNATVA 146
Cdd:COG0492 74 ILLEEVTSVDKDDgpFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGrgvSYCATCDGFFF--------RGKDVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 147 VVGAGLSGVEVASEL-RESRsdlKIYLFDRKDRIlfpypeKLSRY-VEEWFVKHKVTIIRNSNITKVEPN------IVYN 218
Cdd:COG0492 146 VVGGGDSALEEALYLtKFAS---KVTLIHRRDEL------RASKIlVERLRANPKIEVLWNTEVTEIEGDgrvegvTLKN 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446604727 219 HD----EPLECDAIVWTAGIQAN-EVVRNLPVEQDGSGRVVlTKYH---NIPNnehVYVVGDCA 274
Cdd:COG0492 217 VKtgeeKELEVDGVFVAIGLKPNtELLKGLGLELDEDGYIV-VDEDmetSVPG---VFAAGDVR 276
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
145-283 |
2.93e-11 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 64.34 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 145 VAVVGAGLSGVEVASELResRSDLKIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN-----IVYNH 219
Cdd:COG1249 171 LVVIGGGYIGLEFAQIFA--RLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTgdgvtVTLED 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446604727 220 D---EPLECDAIVWTAGIQANevVRNLPVEQ-----DGSGRVVLTKYHNIpNNEHVYVVGDCA---ALPHAPSAQ 283
Cdd:COG1249 249 GggeEAVEADKVLVATGRRPN--TDGLGLEAagvelDERGGIKVDEYLRT-SVPGIYAIGDVTggpQLAHVASAE 320
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
145-214 |
3.90e-11 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 58.37 E-value: 3.90e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 145 VAVVGAGLSGVEVASELRESRSdlKIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN 214
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGS--KVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGN 69
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
91-273 |
1.37e-10 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 62.10 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 91 GGEAIQYDDLIIGLGCEDKYHNVPGAkEYTHSLQSI----EQTRKtyeqlnslepnatVAVVGAGLSGVEVASELRESRS 166
Cdd:PRK06116 126 NGERYTADHILIATGGRPSIPDIPGA-EYGITSDGFfaleELPKR-------------VAVVGAGYIAVEFAGVLNGLGS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 167 DlkIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN------IVYNHDEPLECDAIVWTAGIQANEVV 240
Cdd:PRK06116 192 E--THLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNadgsltLTLEDGETLTVDCLIWAIGREPNTDG 269
|
170 180 190
....*....|....*....|....*....|....*.
gi 446604727 241 RNL---PVEQDGSGRVVLTKYHNIpNNEHVYVVGDC 273
Cdd:PRK06116 270 LGLenaGVKLNEKGYIIVDEYQNT-NVPGIYAVGDV 304
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
2-184 |
8.70e-09 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 56.50 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 2 KHLVILGGGYGGMRILQRLLpsNQLPDDVQVTLIDK-------VPYHcfKTEYYALV---AGTIS--------------E 57
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLL--RRAPEPLRITLFEPrpelgrgVAYS--TDSPEHLLnvpAGRMSafpddpdhflrwlrE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 58 THIRIPFPEHP----------------------------RLNIQYGTVTNIDLEEK--AVHLDGGEAIQYDDLIIGLGce 107
Cdd:COG4529 82 NGARAAPAIDPdafvprrlfgeylrerlaealarapagvRLRHIRAEVVDLERDDGgyRVTLADGETLRADAVVLATG-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 108 dkyHNVPGAkeythsLQSIEQTRKTY-------EQLNSLEPNATVAVVGAGLSGVEVASELRESRSDLKIYLFDRkdRIL 180
Cdd:COG4529 160 ---HPPPAP------PPGLAAGSPRYiadpwppGALARIPPDARVLIIGTGLTAIDVVLSLAARGHRGPITALSR--RGL 228
|
....
gi 446604727 181 FPYP 184
Cdd:COG4529 229 LPRA 232
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
77-274 |
1.75e-08 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 55.31 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 77 VTNIDLEEKAVHLDGgEAIQYDDLIIGLGCEDKYHNVPGaKEYTHSLQSIEQTRKTYEQLNSLEpnaTVAVVGAGLSGVE 156
Cdd:PRK04965 81 VTDIDAEAQVVKSQG-NQWQYDKLVLATGASAFVPPIPG-RELMLTLNSQQEYRAAETQLRDAQ---RVLVVGGGLIGTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 157 VASELreSRSDLKIYLFDRKDRILFPY-PEKLSRYVEEWFVKHKVTIIRNSNITKVEPN-----IVYNHDEPLECDAIVW 230
Cdd:PRK04965 156 LAMDL--CRAGKAVTLVDNAASLLASLmPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTdsgirATLDSGRSIEVDAVIA 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446604727 231 TAGIQANEVV---RNLPVEQDgsgrVVLTKYHNIPNNeHVYVVGDCA 274
Cdd:PRK04965 234 AAGLRPNTALarrAGLAVNRG----IVVDSYLQTSAP-DIYALGDCA 275
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
77-278 |
2.21e-08 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 55.43 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 77 VTNIDLEEKAV---HLDGGEAIQ--YDDLIIGLGCEDKYHNVPGAK-EYTHSLQSIEQTRKTYEQLNSlEPNATVAVVGA 150
Cdd:PRK09564 79 VVKVDAKNKTItvkNLKTGSIFNdtYDKLMIATGARPIIPPIKNINlENVYTLKSMEDGLALKELLKD-EEIKNIVIIGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 151 GLSGVEVASELRESRSDLKIylFDRKDRIL-FPYPEKLSRYVEEWFVKHKV---------TIIRNSNITKVepniVYNHD 220
Cdd:PRK09564 158 GFIGLEAVEAAKHLGKNVRI--IQLEDRILpDSFDKEITDVMEEELRENGVelhlnefvkSLIGEDKVEGV----VTDKG 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446604727 221 EpLECDAIVWTAGIQAN-EVVRNLPVEQDGSGRVVLTKYHNIpNNEHVYVVGDCAALPH 278
Cdd:PRK09564 232 E-YEADVVIVATGVKPNtEFLEDTGLKTLKNGAIIVDEYGET-SIENIYAAGDCATIYN 288
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
77-326 |
1.83e-06 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 49.73 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 77 VTNIDLEEKAVHLDGGEAIQYDDLIIGLGcedKYHNVPGAKEYTHSLQSIeqtRKTYEQLNSLEPNA----TVAVVGAGL 152
Cdd:PRK14989 82 AITINRQEKVIHSSAGRTVFYDKLIMATG---SYPWIPPIKGSETQDCFV---YRTIEDLNAIEACArrskRGAVVGGGL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 153 SGVEVASELRESRSDLKIYLF------DRKDRIlfpYPEKLSRYVEEWFVK-H--KVTIIRNSNITKVEPNIVYNHDEPL 223
Cdd:PRK14989 156 LGLEAAGALKNLGVETHVIEFapmlmaEQLDQM---GGEQLRRKIESMGVRvHtsKNTLEIVQEGVEARKTMRFADGSEL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 224 ECDAIVWTAGIQANEVVRN---LPVEQDGSgrvVLTKYHNIPNNEHVYVVGDCAALPHAPSAQLAEG--QGEQIVQILLK 298
Cdd:PRK14989 233 EVDFIVFSTGIRPQDKLATqcgLAVAPRGG---IVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGykMAQVAVDHLLG 309
|
250 260
....*....|....*....|....*....
gi 446604727 299 RWHNEPLPDELPVIKLKGV-LGSLGKKHG 326
Cdd:PRK14989 310 SENAFEGADLSAKLKLLGVdVGGIGDAHG 338
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
83-273 |
4.06e-06 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 48.46 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 83 EEKAVHLDGGEAIQYDDLIIGLGCEDKYHNVPGaKEYTHSLQSIEQtrktyeqlnsLEPNATVAVVGAGLSGVEVASELR 162
Cdd:PTZ00058 189 SAGVSQLDDGQVIEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFK----------IKEAKRIGIAGSGYIAVELINVVN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 163 esRSDLKIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPN-------IVYNHDEPLECDAIVWTAGIQ 235
Cdd:PTZ00058 258 --RLGAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVkeknltiYLSDGRKYEHFDYVIYCVGRS 335
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446604727 236 ANEVVRNLPVEQDGS--GRVVLTKYHNIpNNEHVYVVGDC 273
Cdd:PTZ00058 336 PNTEDLNLKALNIKTpkGYIKVDDNQRT-SVKHIYAVGDC 374
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
46-271 |
1.35e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 46.06 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 46 EYYALVAgtisethiripfpEHPRLNIQYGT-VTNIDLEEKA--VHLDGGEaIQYDDLIIGLGcEDKYHNVPGAKEYths 122
Cdd:pfam13738 79 EYLRRVA-------------DHFELPINLFEeVTSVKKEDDGfvVTTSKGT-YQARYVIIATG-EFDFPNKLGVPEL--- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 123 lqsieqtRKTYEQLNSLEPNAT--VAVVGAGLSGVEVASELreSRSDLKIYLFDRKDRILFPYPEK---LSRYVEEWF-- 195
Cdd:pfam13738 141 -------PKHYSYVKDFHPYAGqkVVVIGGYNSAVDAALEL--VRKGARVTVLYRGSEWEDRDSDPsysLSPDTLNRLee 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 196 -VKH-KVTIIRNSNITKVE--PNIVYNHDE-----PLECDAIVWTaGIQAN-EVVRNLPVEQDGSGRVVLTKYH---NIP 262
Cdd:pfam13738 212 lVKNgKIKAHFNAEVKEITevDVSYKVHTEdgrkvTSNDDPILAT-GYHPDlSFLKKGLFELDEDGRPVLTEETestNVP 290
|
....*....
gi 446604727 263 NnehVYVVG 271
Cdd:pfam13738 291 G---LFLAG 296
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
56-238 |
3.24e-05 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 45.30 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 56 SETHIRIPFPEH----PRLNIQYG-TVTNIDLEEKAVHLDGGEAIQYDDLIIGLGCEDKYHNVPGA-KEYTHSLQSIEQT 129
Cdd:PRK09754 55 DSPQLQQVLPANwwqeNNVHLHSGvTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDAlGERCFTLRHAGDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 130 RKTYEqlnSLEPNATVAVVGAGLSGVEVASELRESRSdlKIYLFDRKDRILFP-YPEKLSRYVEEWFVKHKVTIIRNSNI 208
Cdd:PRK09754 135 ARLRE---VLQPERSVVIVGAGTIGLELAASATQRRC--KVTVIELAATVMGRnAPPPVQRYLLQRHQQAGVRILLNNAI 209
|
170 180 190
....*....|....*....|....*....|....
gi 446604727 209 TKV----EPNIVYNHDEPLECDAIVWTAGIQANE 238
Cdd:PRK09754 210 EHVvdgeKVELTLQSGETLQADVVIYGIGISAND 243
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
145-277 |
7.20e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 44.40 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 145 VAVVGAGLSGVEVASELreSRSDLKIYLFDRKDRILFPYPEKLSRYVEEWFVK-------HKVTIIRNSNITKVEPNIVY 217
Cdd:PRK06292 172 LAVIGGGVIGLELGQAL--SRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKefkiklgAKVTSVEKSGDEKVEELEKG 249
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446604727 218 NHDEPLECDAIVWTAGIQAN---EVVRNLPVEQDGSGRVVlTKYHNIPNNEHVYVVGDCAALP 277
Cdd:PRK06292 250 GKTETIEADYVLVATGRRPNtdgLGLENTGIELDERGRPV-VDEHTQTSVPGIYAAGDVNGKP 311
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
69-296 |
1.65e-03 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 40.23 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 69 RLNIQYGT-VTNIDLEEKA----VHLDGGEAIQYDDLIIGLGCED--KYHNVPGAKEYT----HSlqsieQTRKTYEQLn 137
Cdd:COG2072 96 RRPIRFGTeVTSARWDEADgrwtVTTDDGETLTARFVVVATGPLSrpKIPDIPGLEDFAgeqlHS-----ADWRNPVDL- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 138 slePNATVAVVGAGLSGVEVASELRESRSDLkiYLFDR------------------KDRILFPYPEKLSRY-VEEWFVKH 198
Cdd:COG2072 170 ---AGKRVLVVGTGASAVQIAPELARVAAHV--TVFQRtppwvlprpnydpergrpANYLGLEAPPALNRRdARAWLRRL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 199 -------------------------------------KVTiIRNSNITKVEPN-IVYNHDEPLECDAIVWTAGIQANEvv 240
Cdd:COG2072 245 lraqvkdpelglltpdyppgckrpllstdyyealrrgNVE-LVTGGIERITEDgVVFADGTEHEVDVIVWATGFRADL-- 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446604727 241 RNLPVEQ--DGSGRVVLTKYH-----NIPNnehVYVVGDCAALPHAPSAQLAEGQGEQIVQIL 296
Cdd:COG2072 322 PWLAPLDvrGRDGRSGPRAYLgvvvpGFPN---LFFLGPNSPSGHSSLTLGAERQARYIARLI 381
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
100-274 |
2.01e-03 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 39.84 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 100 LIIGLGCEDKYHNVPGAKEYthslqSIeqtrkTYEQLNSLE--PNATVaVVGAGLSGVEVASELRESRSDLKIYLfdrKD 177
Cdd:TIGR01438 147 FLIATGERPRYPGIPGAKEL-----CI-----TSDDLFSLPycPGKTL-VVGASYVALECAGFLAGIGLDVTVMV---RS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 178 RILFPYPEKLSRYVEEWFVKHKVTIIRN---SNITKVEPNIVY---NHDEPL--ECDAIVWTAGIQANevVRNLPVEQDG 249
Cdd:TIGR01438 213 ILLRGFDQDCANKVGEHMEEHGVKFKRQfvpIKVEQIEAKVLVeftDSTNGIeeEYDTVLLAIGRDAC--TRKLNLENVG 290
|
170 180 190
....*....|....*....|....*....|...
gi 446604727 250 ------SGRVVLTKYH--NIPnneHVYVVGDCA 274
Cdd:TIGR01438 291 vkinkkTGKIPADEEEqtNVP---YIYAVGDIL 320
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
144-272 |
4.98e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 38.60 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 144 TVAVVGAGLSGVEVASELREsrSDLKIYLFDRKDRIL-FPYPE---KLSRYveewFVKHKVTIIRNSNITKVE--PNIVY 217
Cdd:PRK05249 177 SLIIYGAGVIGCEYASIFAA--LGVKVTLINTRDRLLsFLDDEisdALSYH----LRDSGVTIRHNEEVEKVEggDDGVI 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446604727 218 NHDEP---LECDAIVWTAGIQANEVVRNLP---VEQDGSGRVVLTKYHNIPnNEHVYVVGD 272
Cdd:PRK05249 251 VHLKSgkkIKADCLLYANGRTGNTDGLNLEnagLEADSRGQLKVNENYQTA-VPHIYAVGD 310
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
63-272 |
5.17e-03 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 38.61 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 63 PFPEHPRLNIQYGTVTNIDLEEKAVHLDggeaiQYDDLIIGLGCEdkyHNVPGAK-EYTHSLQSIEQTrktyEQLNSLEP 141
Cdd:PRK13512 77 TYHEVIAINDERQTVTVLNRKTNEQFEE-----SYDKLILSPGAS---ANSLGFEsDITFTLRNLEDT----DAIDQFIK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 142 NATVA---VVGAGLSGVEVASELREsrSDLKIYLFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEPNIVYN 218
Cdd:PRK13512 145 ANQVDkalVVGAGYISLEVLENLYE--RGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTF 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446604727 219 HDEPLE-CDAIVWTAGIQAN-EVVRNLPVEQDGSGRVVLTKYH--NIPNnehVYVVGD 272
Cdd:PRK13512 223 KSGKVEhYDMIIEGVGTHPNsKFIESSNIKLDDKGFIPVNDKFetNVPN---IYAIGD 277
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
145-283 |
9.29e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 37.82 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 145 VAVVGAGLSGVEVASELRESRSDLKIylFDRKDRILFPYPEKLSRYVEEWFVKHKVTIIRNSNITKVEP--NIVYNHDEP 222
Cdd:PRK06416 175 LVVIGGGYIGVEFASAYASLGAEVTI--VEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQtdDGVTVTLED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446604727 223 ------LECDAIVWTAGIQAN-----------EVVRNLpVEQDGSGRVvltkyhNIPnneHVYVVGDCAA---LPHAPSA 282
Cdd:PRK06416 253 ggkeetLEADYVLVAVGRRPNtenlgleelgvKTDRGF-IEVDEQLRT------NVP---NIYAIGDIVGgpmLAHKASA 322
|
.
gi 446604727 283 Q 283
Cdd:PRK06416 323 E 323
|
|
|