|
Name |
Accession |
Description |
Interval |
E-value |
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
76-355 |
4.04e-37 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 137.96 E-value: 4.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 76 NFRQGLVVGIDLKNQMVLLQGGEALPFSHLILATGSTGPFPGkfNE--------VSSQQAAIQAYEDMVRQVQRS----- 142
Cdd:COG1252 72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG--IPglaehalpLKTLEDALALRERLLAAFERAerrrl 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 143 -RF---------IvvvgggsagvEMAAEI------KTEYPEK-----EVTLIHsqvalADKELLP----SVRQEVKEILL 197
Cdd:COG1252 150 lTIvvvgggptgV----------ELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 198 RKGVQLLLSERVSNLEELplneyreyiKVQTDKGTEVATNLVILCTGIKINSSAYRKAFEsrLASSGALRVNEHLQVEGH 277
Cdd:COG1252 215 KRGVEVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 278 SNVYAIGDCADVR------TPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGALTFLLSMGRNDGVGQISGFYVGRLMV 351
Cdd:COG1252 284 PNVFAIGDCAAVPdpdgkpVPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLA 363
|
....
gi 23273801 352 RLTK 355
Cdd:COG1252 364 WLLK 367
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
77-310 |
1.92e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 76.88 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 77 FRQGLVVGIDLKNQMVLLQGgEALPFSHLILATGSTG---PFPGkfNEV----SSQQAaIQAYEDMVRQVQRsrfIVVVG 149
Cdd:PRK04965 76 FPHTWVTDIDAEAQVVKSQG-NQWQYDKLVLATGASAfvpPIPG--RELmltlNSQQE-YRAAETQLRDAQR---VLVVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 150 GGSAGVEMAAEIKTEypEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELplneyREYIKVQTD 229
Cdd:PRK04965 149 GGLIGTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 230 KGTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVEgHSNVYAIGDCADVRTPKMAYL--AGLHANIAVA 307
Cdd:PRK04965 222 SGRSIEVDAVIAAAGLRPNTAL---ARRAGLAVNRGIVVDSYLQTS-APDIYALGDCAEINGQVLPFLqpIQLSAMALAK 297
|
...
gi 23273801 308 NIV 310
Cdd:PRK04965 298 NLL 300
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
19-302 |
1.50e-07 |
|
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: 52.32 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 19 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVETGFAKKTFISYSVTFK---DNFRQGL-------VVG 84
Cdd:pfam07992 8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEevvKKLNNGIevllgteVVS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 85 IDLKNQMVLLQ-----GGEALPFSHLILATGSTG---PFPGKFNEVSSQQAAIQAYEDMVRQVQRSR-------FIvvvg 149
Cdd:pfam07992 88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPGVELNVGFLVRTLDSAEALRLKLLPKRvvvvgggYI---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 150 ggsaGVEMAAEIkTEYPeKEVTLIHSQVALAdKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPlneyrEYIKVQTD 229
Cdd:pfam07992 164 ----GVELAAAL-AKLG-KEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDG-----DGVEVILK 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23273801 230 KGTEVATNLVILCTGIKINSSAYRKA-FEsrLASSGALRVNEHLQVEgHSNVYAIGDCaDVRTPKMAYLAGLHA 302
Cdd:pfam07992 232 DGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
82-290 |
1.30e-06 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 50.21 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 82 VVGIDLKNQMVLLQGGEALPFSHLILATGSTG---PFPGkfnevSSQQAA--------IQAYEDMVRQVQRSRFIVVVGG 150
Cdd:TIGR02374 77 VIQIDTDQKQVITDAGRTLSYDKLILATGSYPfilPIPG-----ADKKGVyvfrtiedLDAIMAMAQRFKKAAVIGGGLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 151 GsagveMAAEIKTEYPEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSErvsNLEELPLNEYREYIKVQtdK 230
Cdd:TIGR02374 152 G-----LEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--D 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 231 GTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVEgHSNVYAIGDCADVR 290
Cdd:TIGR02374 222 GSSLEADLIVMAAGIRPNDEL---AVSAGIKVNRGIIVNDSMQTS-DPDIYAVGECAEHN 277
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
76-355 |
4.04e-37 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 137.96 E-value: 4.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 76 NFRQGLVVGIDLKNQMVLLQGGEALPFSHLILATGSTGPFPGkfNE--------VSSQQAAIQAYEDMVRQVQRS----- 142
Cdd:COG1252 72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG--IPglaehalpLKTLEDALALRERLLAAFERAerrrl 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 143 -RF---------IvvvgggsagvEMAAEI------KTEYPEK-----EVTLIHsqvalADKELLP----SVRQEVKEILL 197
Cdd:COG1252 150 lTIvvvgggptgV----------ELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 198 RKGVQLLLSERVSNLEELplneyreyiKVQTDKGTEVATNLVILCTGIKINSSAYRKAFEsrLASSGALRVNEHLQVEGH 277
Cdd:COG1252 215 KRGVEVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 278 SNVYAIGDCADVR------TPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGALTFLLSMGRNDGVGQISGFYVGRLMV 351
Cdd:COG1252 284 PNVFAIGDCAAVPdpdgkpVPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLA 363
|
....
gi 23273801 352 RLTK 355
Cdd:COG1252 364 WLLK 367
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
64-310 |
2.70e-24 |
|
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: 101.43 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 64 KTFISYSVTFKdnfRQGLVVGIDLKNQMVLLQGGEALPFSHLILATGST---GPFPG-KFNEVSSqqaaIQAYEDMVR-- 137
Cdd:COG0446 44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPGlDLPGVFT----LRTLDDADAlr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 138 ------QVQR-----SRFIvvvgggsaGVEMAAEIKTEypEKEVTLIH--SQV-ALADKEllpsVRQEVKEILLRKGVQL 203
Cdd:COG0446 117 ealkefKGKRavvigGGPI--------GLELAEALRKR--GLKVTLVEraPRLlGVLDPE----MAALLEEELREHGVEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 204 LLSERVSNLEElplneyREYIKVQTDKGTEVATNLVILCTGIKINSSAyrkAFESRLA--SSGALRVNEHLQVeGHSNVY 281
Cdd:COG0446 183 RLGETVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPNTEL---AKDAGLAlgERGWIKVDETLQT-SDPDVY 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 23273801 282 AIGDCADVR---TPKMAYLA-GLHAN----IAVANIV 310
Cdd:COG0446 253 AAGDCAEVPhpvTGKTVYIPlASAANkqgrVAAENIL 289
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
82-310 |
1.83e-15 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 77.10 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 82 VVGIDLKNQMVLLQGGEALPFSHLILATGSTgPF----PGkfnevsSQQAAIQAY------EDMVRQVQRSR-------- 143
Cdd:COG1251 79 VTAIDRAARTVTLADGETLPYDKLVLATGSR-PRvppiPG------ADLPGVFTLrtlddaDALRAALAPGKrvvviggg 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 144 FIvvvgggsaGVEMAAEIKTEypEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEElplNEYREy 223
Cdd:COG1251 152 LI--------GLEAAAALRKR--GLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG---DDRVT- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 224 iKVQTDKGTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVeGHSNVYAIGDCADVRTPkmayLAGLHAN 303
Cdd:COG1251 218 -GVRLADGEELPADLVVVAIGVRPNTEL---ARAAGLAVDRGIVVDDYLRT-SDPDIYAAGDCAEHPGP----VYGRRVL 288
|
....*..
gi 23273801 304 IAVANIV 310
Cdd:COG1251 289 ELVAPAY 295
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
77-310 |
1.92e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 76.88 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 77 FRQGLVVGIDLKNQMVLLQGgEALPFSHLILATGSTG---PFPGkfNEV----SSQQAaIQAYEDMVRQVQRsrfIVVVG 149
Cdd:PRK04965 76 FPHTWVTDIDAEAQVVKSQG-NQWQYDKLVLATGASAfvpPIPG--RELmltlNSQQE-YRAAETQLRDAQR---VLVVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 150 GGSAGVEMAAEIKTEypEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELplneyREYIKVQTD 229
Cdd:PRK04965 149 GGLIGTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 230 KGTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVEgHSNVYAIGDCADVRTPKMAYL--AGLHANIAVA 307
Cdd:PRK04965 222 SGRSIEVDAVIAAAGLRPNTAL---ARRAGLAVNRGIVVDSYLQTS-APDIYALGDCAEINGQVLPFLqpIQLSAMALAK 297
|
...
gi 23273801 308 NIV 310
Cdd:PRK04965 298 NLL 300
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
77-344 |
6.73e-12 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 66.33 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 77 FRQGLVVGIDLKNQMVL----------LQGGEALPFSHLILATGSTgpfPGKFNevssqqaaIQAYEDMV---RQVQRSR 143
Cdd:PTZ00318 79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAfflKEVNHAR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 144 FIVVVGGGSAgveMAAEIKTEYPEKEVTLIHSQVA------------LAD------KELLPSVRQEVKEILLRKGVQLLL 205
Cdd:PTZ00318 148 GIRKRIVQCI---ERASLPTTSVEERKRLLHFVVVgggptgvefaaeLADffrddvRNLNPELVEECKVTVLEAGSEVLG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 206 S--ERVSNLEELPLNEYREYIKVQ------------TDKGTEVATNLVILCTGIkiNSSAYRKAFESRLASSGALRVNEH 271
Cdd:PTZ00318 225 SfdQALRKYGQRRLRRLGVDIRTKtavkevldkevvLKDGEVIPTGLVVWSTGV--GPGPLTKQLKVDKTSRGRISVDDH 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23273801 272 LQVEGHSNVYAIGDCADVRT---PKMAYLAGLHANIAVANIVNSVKQRPLQayKPGALTFLLSM---GRNDGVGQISGF 344
Cdd:PTZ00318 303 LRVKPIPNVFALGDCAANEErplPTLAQVASQQGVYLAKEFNNELKGKPMS--KPFVYRSLGSLaylGNYSAIVQLGAF 379
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
156-289 |
1.59e-11 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 65.45 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 156 EMAAEIKTEypEKEVTLI-HSQVALA---DKELLPSVRQEVKEillrKGVQLLLSERVSNLEelplNEYREYiKVQTDKG 231
Cdd:PRK09564 163 EAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSLI----GEDKVE-GVVTDKG 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23273801 232 tEVATNLVILCTGIKINSSAYRKAFESRLAsSGALRVNEhlqvEGHS---NVYAIGDCADV 289
Cdd:PRK09564 232 -EYEADVVIVATGVKPNTEFLEDTGLKTLK-NGAIIVDE----YGETsieNIYAAGDCATI 286
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
92-311 |
2.43e-08 |
|
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: 55.48 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 92 VLLQGGEALPFSHLILATGSTG---PFPGKFNE--VSSQQAaiqayEDMVRQVQR-----SRFIvvvgggsaGVEMA--- 158
Cdd:COG1249 121 VEVTGGETLTADHIVIATGSRPrvpPIPGLDEVrvLTSDEA-----LELEELPKSlvvigGGYI--------GLEFAqif 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 159 AEIKTeypekEVTLIHSQ---VALADKEllpsVRQEVKEILLRKGVQLLLSERVSNLEELPlneyrEYIKVQTDKGTEVA 235
Cdd:COG1249 188 ARLGS-----EVTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DGVTVTLEDGGGEE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 236 TN---LVILCTGIKINSSAYrkAFES---RLASSGALRVNEHLQVeGHSNVYAIGDCADvrTPKMAYLAGLHANIAVANI 309
Cdd:COG1249 254 AVeadKVLVATGRRPNTDGL--GLEAagvELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GPQLAHVASAEGRVAAENI 328
|
..
gi 23273801 310 VN 311
Cdd:COG1249 329 LG 330
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
19-302 |
1.50e-07 |
|
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: 52.32 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 19 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVETGFAKKTFISYSVTFK---DNFRQGL-------VVG 84
Cdd:pfam07992 8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEevvKKLNNGIevllgteVVS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 85 IDLKNQMVLLQ-----GGEALPFSHLILATGSTG---PFPGKFNEVSSQQAAIQAYEDMVRQVQRSR-------FIvvvg 149
Cdd:pfam07992 88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPGVELNVGFLVRTLDSAEALRLKLLPKRvvvvgggYI---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 150 ggsaGVEMAAEIkTEYPeKEVTLIHSQVALAdKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPlneyrEYIKVQTD 229
Cdd:pfam07992 164 ----GVELAAAL-AKLG-KEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDG-----DGVEVILK 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23273801 230 KGTEVATNLVILCTGIKINSSAYRKA-FEsrLASSGALRVNEHLQVEgHSNVYAIGDCaDVRTPKMAYLAGLHA 302
Cdd:pfam07992 232 DGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
82-290 |
1.30e-06 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 50.21 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 82 VVGIDLKNQMVLLQGGEALPFSHLILATGSTG---PFPGkfnevSSQQAA--------IQAYEDMVRQVQRSRFIVVVGG 150
Cdd:TIGR02374 77 VIQIDTDQKQVITDAGRTLSYDKLILATGSYPfilPIPG-----ADKKGVyvfrtiedLDAIMAMAQRFKKAAVIGGGLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 151 GsagveMAAEIKTEYPEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSErvsNLEELPLNEYREYIKVQtdK 230
Cdd:TIGR02374 152 G-----LEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--D 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 231 GTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVEgHSNVYAIGDCADVR 290
Cdd:TIGR02374 222 GSSLEADLIVMAAGIRPNDEL---AVSAGIKVNRGIIVNDSMQTS-DPDIYAVGECAEHN 277
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
96-309 |
1.34e-06 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 49.95 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 96 GGEALPFSHLILATGS-----TGPFPGKFNEVSSQQAAIQayedmVRQVQRSRFIVVvgggsagvemAAEIKTEYPE--- 167
Cdd:TIGR01350 126 GEETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESLVIIG----------GGVIGIEFASifa 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23273801 168 ---KEVTLIHSQvaladKELLP----SVRQEVKEILLRKGVQLLLSERVSNLEELplneyREYIKVQTDKGTEVAT--NL 238
Cdd:TIGR01350 191 slgSKVTVIEML-----DRILPgedaEVSKVLQKALKKKGVKILTNTKVTAVEKN-----DDQVTYENKGGETETLtgEK 260
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23273801 239 VILCTGIKINSSAY-RKAFESRLASSGALRVNEHLQVeGHSNVYAIGDCadVRTPKMAYLAGLHANIAVANI 309
Cdd:TIGR01350 261 VLVAVGRKPNTEGLgLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDV--IGGPMLAHVASHEGIVAAENI 329
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
210-285 |
4.00e-03 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 39.03 E-value: 4.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23273801 210 SNLEELPLNEyrEYIKVQTDKGTEVATNLVILCTGIKINSSAYR-KAFESRLASSGALRVNEHLQVEGHSnVYAIGD 285
Cdd:PLN02507 265 TNLTQLTKTE--GGIKVITDHGEEFVADVVLFATGRAPNTKRLNlEAVGVELDKAGAVKVDEYSRTNIPS-IWAIGD 338
|
|
|