|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
4-368 |
5.17e-116 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 343.28 E-value: 5.17e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 4 RAPLVIIGTGLAGYNLAREWRKLDGETPLLMITADDGRSYSKPMLSTGFSKNKDADGLAMAePGAMAEQLNARILTHTRV 83
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLR-PADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 84 TGIDPGHQRIWIGE-EEVRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKRRVLLLGAGLIGCEFAN 162
Cdd:COG1251 80 TAIDRAARTVTLADgETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 163 DLSSGGYQLDVVAPCEQVMPGLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIPCDLVVSAVGLR 242
Cdd:COG1251 160 ALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 243 PRTELAFAAGLAVNRGIVVDRSLRTSHANIYALGDCAEVDG-----LNLLYVMPLMACARALAQTLAGNPSQVAYGPMPV 317
Cdd:COG1251 240 PNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGpvygrRVLELVAPAYEQARVAAANLAGGPAAYEGSVPST 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15600542 318 TVKTPACPLVVSPPPRGMDG--QWLVEGSGTDLKVLCRDtaGRVIGYALTGAA 368
Cdd:COG1251 320 KLKVFGVDVASAGDAEGDEEvvVRGDPARGVYKKLVLRD--GRLVGAVLVGDT 370
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
1-380 |
2.94e-110 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 327.64 E-value: 2.94e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 1 MSerAPLVIIGTGLAGYNLAREWRKLDGETPLLMITADDGRSYSKPMLSTGFSKNKDADGLAMAEPGAMAEQLNARILTH 80
Cdd:PRK04965 1 MS--NGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDLTRQSAGEFAEQFNLRLFPH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 81 TRVTGIDPGHQRIWIGEEEVRYRDLVLAWGAEPIRVPVEGDAQdaLYPINDLEDYARFRQAAAGKRRVLLLGAGLIGCEF 160
Cdd:PRK04965 79 TWVTDIDAEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGREL--MLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 161 ANDLSSGGYQLDVVAPCEQVMPGLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIPCDLVVSAVG 240
Cdd:PRK04965 157 AMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 241 LRPRTELAFAAGLAVNRGIVVDRSLRTSHANIYALGDCAEVDGLNLLYVMPLMACARALAQTLAGNPSQVAYGPMPVTVK 320
Cdd:PRK04965 237 LRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQPIQLSAMALAKNLLGQNTPLKLPAMLVKVK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 321 TPACPLVVSPPPRGMDGQWLVEGSGTDLKVLCRDTAGRVIGYALTGAAVNEKLALNKELP 380
Cdd:PRK04965 317 TPELPLQLAGETQRQDLRWQINAESQGMVAKGVDEAGQLRAFVVSEDRMKEAFPLLKELP 376
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
25-307 |
1.60e-53 |
|
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: 180.01 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 25 KLDGETPLLMITADDGRSYSKPMLSTGFSKN-KDADGLAMAEPGAMAEQlNARILTHTRVTGIDPGHQRIWI-GEEEVRY 102
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGiKDPEDLLVRTPESFERK-GIDVRTGTEVTAIDPEAKTVTLrDGETLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 103 RDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGK--RRVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQV 180
Cdd:COG0446 80 DKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFkgKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 181 MPGLLhPAAAKAVQAGLEGLGVRFHLGPVLASLKkAGEGLEAHLSDGEVIPCDLVVSAVGLRPRTELAFAAGLAVNR--G 258
Cdd:COG0446 160 LGVLD-PEMAALLEEELREHGVELRLGETVVAID-GDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgW 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15600542 259 IVVDRSLRTSHANIYALGDCAEVDG--LNLLYVMPLMA----CARALAQTLAGNP 307
Cdd:COG0446 238 IKVDETLQTSDPDVYAAGDCAEVPHpvTGKTVYIPLASaankQGRVAAENILGGP 292
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
7-278 |
6.76e-49 |
|
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: 167.11 E-value: 6.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 7 LVIIGTGLAGYNLAREWRKLDGETplLMITADDGRSYSKPMLSTGFSKNKDADGLAMAEPGAMA------EQLNARI--L 78
Cdd:pfam07992 3 VVVIGGGPAGLAAALTLAQLGGKV--TLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKrkeevvKKLNNGIevL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 79 THTRVTGIDPGHQRIWI------GEEEVRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKRrVLLLG 152
Cdd:pfam07992 81 LGTEVVSIDPGAKKVVLeelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKR-VVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 153 AGLIGCEFANDLSSGGYQLDVVAPCEQVMPGLLhPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIPC 232
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLLRAFD-EEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15600542 233 DLVVSAVGLRPRTELAFAAGLAVNR--GIVVDRSLRTSHANIYALGDC 278
Cdd:pfam07992 239 DLVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDC 286
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
7-318 |
1.31e-48 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 175.40 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 7 LVIIGTGLAGYNLAREWRKLDGETPLLMITADDGR-SYSKPMLSTGFSKNKDADGLAMAEPGaMAEQLNARILTHTRVTG 85
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHMFEITIFGEEPHpNYNRILLSSVLQGEADLDDITLNSKD-WYEKHGITLYTGETVIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 86 IDPGHQRIWIGEEE-VRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKRRVLLLGAGLIGCEFANDL 164
Cdd:TIGR02374 80 IDTDQKQVITDAGRtLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 165 SSGGYQLDVVAPCEQVMPGLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIPCDLVVSAVGLRPR 244
Cdd:TIGR02374 160 QNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600542 245 TELAFAAGLAVNRGIVVDRSLRTSHANIYALGDCAEVDGLNLLYVMPLMACARALAQTLAGNPSQVAYGPMPVT 318
Cdd:TIGR02374 240 DELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICGVECEEYEGSDLSA 313
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
7-307 |
7.58e-29 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 115.61 E-value: 7.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 7 LVIIGTGLAGYNLAREWRK-LDGETPLLMITADDgRSYSKPML---STGFsknKDADGLAMaEPGAMAEQLNARILtHTR 82
Cdd:COG1252 4 IVIVGGGFAGLEAARRLRKkLGGDAEVTLIDPNP-YHLFQPLLpevAAGT---LSPDDIAI-PLRELLRRAGVRFI-QGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 83 VTGIDPGHQRIWIGE-EEVRYRDLVLAWGAEPIRVPVEGDAQDA--LYPINDLEDY-----ARFRQAAAGKR-RVLLLGA 153
Cdd:COG1252 78 VTGIDPEARTVTLADgRTLSYDYLVIATGSVTNFFGIPGLAEHAlpLKTLEDALALrerllAAFERAERRRLlTIVVVGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 154 GLIGCEFA-------------NDLSSGGYQLDVVAPCEQVMPGLlHPAAAKAVQAGLEGLGVRFHLGpvlASLKKAGEGl 220
Cdd:COG1252 158 GPTGVELAgelaellrkllryPGIDPDKVRITLVEAGPRILPGL-GEKLSEAAEKELEKRGVEVHTG---TRVTEVDAD- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 221 EAHLSDGEVIPCDLVVSAVGLRPRTELAfAAGLAVNRG--IVVDRSLRT-SHANIYALGDCAEVDGLNLLYVMPL----- 292
Cdd:COG1252 233 GVTLEDGEEIPADTVIWAAGVKAPPLLA-DLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCAAVPDPDGKPVPKTaqaav 311
|
330
....*....|....*...
gi 15600542 293 -MA--CARALAQTLAGNP 307
Cdd:COG1252 312 qQAkvLAKNIAALLRGKP 329
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
96-316 |
3.36e-28 |
|
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: 114.80 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 96 GEEEVRYRDLVLAWGAEPIRVPVEG-------DAQDALypinDLEDYarfrqaaagKRRVLLLGAGLIGCEFANDLSSGG 168
Cdd:COG1249 125 GGETLTADHIVIATGSRPRVPPIPGldevrvlTSDEAL----ELEEL---------PKSLVVIGGGYIGLEFAQIFARLG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 169 YQLDVVAPCEQVMPGLlHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDG---EVIPCDLVVSAVGLRPRT 245
Cdd:COG1249 192 SEVTLVERGDRLLPGE-DPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGggeEAVEADKVLVATGRRPNT 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600542 246 E---LAfAAGLAVNR--GIVVDRSLRTSHANIYALGDCaeVDGLNLLYVMplMACARALAQTLAGNPSQ-VAYGPMP 316
Cdd:COG1249 271 DglgLE-AAGVELDErgGIKVDEYLRTSVPGIYAIGDV--TGGPQLAHVA--SAEGRVAAENILGKKPRpVDYRAIP 342
|
|
| Rbx_binding |
pfam18113 |
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin ... |
309-379 |
2.51e-27 |
|
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin reductase (RdxR) present in Pseudomonas aeruginosa. RdxR are important in prokaryotes as they allow for the metabolism of inert n-alkanes and RdxR is also crucial for archaea and anaerobic bacteria in the response to oxidative stress. This domain is known to recognize and bind to rubredoxin.
Pssm-ID: 436282 Cd Length: 71 Bit Score: 103.09 E-value: 2.51e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600542 309 QVAYGPMPVTVKTPACPLVVSPPPRGMDGQWLVEGSGTDLKVLCRDTAGRVIGYALTGAAVNEKLALNKEL 379
Cdd:pfam18113 1 AVVYPAMPVIVKTPACPLVVAPPAVGAEGEWQIEGDGEGLTARFYDADGQLLGFALTGEAVAQRMALLKQL 71
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
7-279 |
3.20e-23 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 100.00 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 7 LVIIGTGLAGYNLAREWRK--LDGEtpLLMITADDGRSYSKPMLSTGFSKNkDADGLAMAEPGAMAEQLNARILTHTRVT 84
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQqgFTGE--LHLFSDERHLPYERPPLSKSMLLE-DSPQLQQVLPANWWQENNVHLHSGVTIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 85 GIDPG-HQRIWIGEEEVRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKRRVLLLGAGLIGCEFAND 163
Cdd:PRK09754 83 TLGRDtRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 164 LSSGGYQLDVVAPCEQVMPGLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKaGEGLEAHLSDGEVIPCDLVVSAVGLRP 243
Cdd:PRK09754 163 ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVD-GEKVELTLQSGETLQADVVIYGIGISA 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 15600542 244 RTELAFAAGLAVNRGIVVDRSLRTSHANIYALGDCA 279
Cdd:PRK09754 242 NDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVA 277
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
7-320 |
9.59e-23 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 100.19 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 7 LVIIGTGLAGYNLAREW-RKLDGETPLLMITADDGR-SYSKPMLSTGFSKNKdADGLAMAEPGaMAEQLNARILTHTRVT 84
Cdd:PRK14989 6 LAIIGNGMVGHRFIEDLlDKADAANFDITVFCEEPRiAYDRVHLSSYFSHHT-AEELSLVREG-FYEKHGIKVLVGERAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 85 GIDPGHQRIWIGE-EEVRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKRRVLLLGAGLIGCEFAND 163
Cdd:PRK14989 84 TINRQEKVIHSSAgRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEAAGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 164 LSSGGYQLDVVAPCEQVMPGLLHPAAAKAVQAGLEGLGVRFHLGPvlASLKKAGEGLEAH----LSDGEVIPCDLVVSAV 239
Cdd:PRK14989 164 LKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSK--NTLEIVQEGVEARktmrFADGSELEVDFIVFST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 240 GLRPRTELAFAAGLAVNR--GIVVDRSLRTSHANIYALGDCAEVDGLNLLYVMPLMACARALAQTLAGNPSQVAYGPMPV 317
Cdd:PRK14989 242 GIRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGSENAFEGADLSA 321
|
...
gi 15600542 318 TVK 320
Cdd:PRK14989 322 KLK 324
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
7-306 |
5.06e-21 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 93.95 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 7 LVIIGTGLAGYNLAREWRKLDGETPLLMITADDGRSYSK---PMLSTGFSKNkdADGLAMAEPGAMAEQ-LNARilTHTR 82
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGAcglPYFVGGFFDD--PNTMIARTPEEFIKSgIDVK--TEHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 83 VTGIDPGHQRIWI---GEEEV---RYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKR--RVLLLGAG 154
Cdd:PRK09564 79 VVKVDAKNKTITVknlKTGSIfndTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEikNIVIIGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 155 LIGCEFANDLSSGGYQLDVVAPCEQVMPGLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKkAGEGLEAHLSDGEVIPCDL 234
Cdd:PRK09564 159 FIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLI-GEDKVEGVVTDKGEYEADV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 235 VVSAVGLRPRTELAFAAGL--AVNRGIVVDRSLRTSHANIYALGDCAEVDGLNL---LYVmPLMACA----RALAQTLAG 305
Cdd:PRK09564 238 VIVATGVKPNTEFLEDTGLktLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSnknVYV-PLATTAnklgRMVGENLAG 316
|
.
gi 15600542 306 N 306
Cdd:PRK09564 317 R 317
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
96-316 |
1.69e-20 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 92.52 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 96 GEEEVRYRDLVLAWGAEPIRVP---VEG----DAQDALypinDLEDYARfrqaaagkrRVLLLGAGLIGCEFANDLSSGG 168
Cdd:PRK06416 129 GEQTYTAKNIILATGSRPRELPgieIDGrviwTSDEAL----NLDEVPK---------SLVVIGGGYIGVEFASAYASLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 169 YQLDVVAPCEQVMPGLlHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDG---EVIPCDLVVSAVGLRPRT 245
Cdd:PRK06416 196 AEVTIVEALPRILPGE-DKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVTVTLEDGgkeETLEADYVLVAVGRRPNT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 246 E-LAF-AAGLAVNRG-IVVDRSLRTSHANIYALGDCAEvdglnllyvmPLMACARALAQ------TLAGNPSQVAYGPMP 316
Cdd:PRK06416 275 EnLGLeELGVKTDRGfIEVDEQLRTNVPNIYAIGDIVG----------GPMLAHKASAEgiiaaeAIAGNPHPIDYRGIP 344
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
146-306 |
1.84e-16 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 80.59 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 146 RRVLLLGAGLIGCEFANDLSSGGYQLDvvapceqvmpgLLH----------PAAAKAVQAGLEGLGVRFHLGPVLASLKK 215
Cdd:PRK06116 168 KRVAVVGAGYIAVEFAGVLNGLGSETH-----------LFVrgdaplrgfdPDIRETLVEEMEKKGIRLHTNAVPKAVEK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 216 AGEG-LEAHLSDGEVIPCDLVVSAVGLRPRTE---LAfAAGLAVN-RG-IVVDRSLRTSHANIYALGDCAevDGLNLLYV 289
Cdd:PRK06116 237 NADGsLTLTLEDGETLTVDCLIWAIGREPNTDglgLE-NAGVKLNeKGyIIVDEYQNTNVPGIYAVGDVT--GRVELTPV 313
|
170
....*....|....*..
gi 15600542 290 MplMACARALAQTLAGN 306
Cdd:PRK06116 314 A--IAAGRRLSERLFNN 328
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
89-278 |
2.67e-15 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 77.16 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 89 GHQRIWIGEEEVRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFrqaaagKRRVLLLGAGLIGCEFANDLSSGG 168
Cdd:PRK06370 121 SPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDEVGYLTNETIFSLDEL------PEHLVIIGGGYIGLEFAQMFRRFG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 169 YQLDVVapceQVMPGLLH---PAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHL---SDGEVIPCDLVVSAVGLR 242
Cdd:PRK06370 195 SEVTVI----ERGPRLLPredEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLdcnGGAPEITGSHILVAVGRV 270
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600542 243 PRTE---LAfAAGLAVNR--GIVVDRSLRTSHANIYALGDC 278
Cdd:PRK06370 271 PNTDdlgLE-AAGVETDArgYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
7-280 |
2.12e-14 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 74.05 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 7 LVIIGTGLAGYNLAREWRKLDGETPLLMITADDGRSYSKPMLSTGFSKN-KDADGLAMAEPGAMAEQLNARILTHTRVTG 85
Cdd:PRK13512 4 IIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVvEDRKYALAYTPEKFYDRKQITVKTYHEVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 86 IDPGHQRIWIGEE------EVRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKRrVLLLGAGLIGCE 159
Cdd:PRK13512 84 INDERQTVTVLNRktneqfEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDK-ALVVGAGYISLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 160 FANDLSSGGYQLDVVAPCEQVMPgLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKkageGLEAHLSDGEVIPCDLVVSAV 239
Cdd:PRK13512 163 VLENLYERGLHPTLIHRSDKINK-LMDADMNQPILDELDKREIPYRLNEEIDAIN----GNEVTFKSGKVEHYDMIIEGV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15600542 240 GLRPRTELAFAAGLAVNRG--IVVDRSLRTSHANIYALGDCAE 280
Cdd:PRK13512 238 GTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIIT 280
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
96-289 |
1.79e-13 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 71.30 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 96 GEEEVRYRDLVL-AWGAEPIRVPVEGdAQDALYPINDledyarfrQAAAGKR---RVLLLGAGLIGCEFANDLSSGGYQL 171
Cdd:TIGR02053 122 LGREVRGAKRFLiATGARPAIPPIPG-LKEAGYLTSE--------EALALDRipeSLAVIGGGAIGVELAQAFARLGSEV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 172 DVVAPCEQVMPGLlHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHL----SDGEVIPCDLVVsAVGLRPRTE- 246
Cdd:TIGR02053 193 TILQRSDRLLPRE-EPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVekpgGQGEVEADELLV-ATGRRPNTDg 270
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600542 247 LAF-AAGLAVNR--GIVVDRSLRTSHANIYALGDCaeVDGLNLLYV 289
Cdd:TIGR02053 271 LGLeKAGVKLDErgGILVDETLRTSNPGIYAAGDV--TGGLQLEYV 314
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
70-279 |
3.23e-13 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 69.76 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 70 AEQLNARILThTRVTGIDPgHQRIWI----GEEEVRYRDLVLAWGAEPIRVPVEGdaqdalypINDLEDY---------- 135
Cdd:COG0492 67 AERFGAEILL-EEVTSVDK-DDGPFRvttdDGTEYEAKAVIIATGAGPRKLGLPG--------EEEFEGRgvsycatcdg 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 136 ARFRqaaagKRRVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQVMpgllhpaAAKAVQAGLEGL-GVRFHLGPVLASLK 214
Cdd:COG0492 137 FFFR-----GKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELR-------ASKILVERLRANpKIEVLWNTEVTEIE 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600542 215 KAG--EGLE-AHLSDGEV--IPCDLVVSAVGLRPRTELAFAAGLAVNRG--IVVDRSLRTSHANIYALGDCA 279
Cdd:COG0492 205 GDGrvEGVTlKNVKTGEEkeLEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVR 276
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
7-319 |
3.47e-13 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 70.59 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 7 LVIIGTGLAGYNLAREWRKL-------DGETP-------------LLMITADD----------GRSYSKPMLSTGFS--- 53
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLgkkvaliEKGPLggtclnvgcipskALIAAAEAfheakhaeefGIHADGPKIDFKKVmar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 54 KNKDADGLAmaepGAMAEQLNArILTHTRVTG----IDPGhqRIWIGEEEVRYRDLVLAWGAEPIRVP-VEGDAQDALYP 128
Cdd:PRK06292 86 VRRERDRFV----GGVVEGLEK-KPKIDKIKGtarfVDPN--TVEVNGERIEAKNIVIATGSRVPPIPgVWLILGDRLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 129 INDLedyarFRQAAAGKRrVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQVMPgLLHPAAAKAVQAGLEGlGVRFHLG- 207
Cdd:PRK06292 159 SDDA-----FELDKLPKS-LAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSK-EFKIKLGa 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 208 PVLASLKKAGEGLEAHLSDGEV--IPCDLVVSAVGLRPRTE-LAFA-AGLAV-NRG-IVVDRSLRTSHANIYALGDcaeV 281
Cdd:PRK06292 231 KVTSVEKSGDEKVEELEKGGKTetIEADYVLVATGRRPNTDgLGLEnTGIELdERGrPVVDEHTQTSVPGIYAAGD---V 307
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15600542 282 DGlnllyVMPLMACA----RALAQTLAGNPSQ-VAYGPMPVTV 319
Cdd:PRK06292 308 NG-----KPPLLHEAadegRIAAENAAGDVAGgVRYHPIPSVV 345
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
80-277 |
5.30e-13 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 69.98 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 80 HTRVTGidpgHQRIWIGE-EEVRYRDLVLAWGAEPIRVPVEGDAqDALYPINDleDYARFRQAAagkRRVLLLGAGLIGC 158
Cdd:PRK07846 110 HARFIG----PKTLRTGDgEEITADQVVIAAGSRPVIPPVIADS-GVRYHTSD--TIMRLPELP---ESLVIVGGGFIAA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 159 EFANDLSSGGYQLDVVAPCEQvmpgLLHPAAAKAVQAGLEGLGVRF--HLGPVLASLKKAGEGLEAHLSDGEVIPCDLVV 236
Cdd:PRK07846 180 EFAHVFSALGVRVTVVNRSGR----LLRHLDDDISERFTELASKRWdvRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600542 237 SAVGLRPRTEL--AFAAGLAVNRG--IVVDRSLRTSHANIYALGD 277
Cdd:PRK07846 256 VATGRVPNGDLldAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGD 300
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
146-277 |
1.51e-12 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 68.64 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 146 RRVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQVMPgLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLS 225
Cdd:PRK05249 176 RSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLK 254
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600542 226 DGEVIPCDLVVSAVGLRPRTE---LAfAAGLAVN-RG-IVVDRSLRTSHANIYALGD 277
Cdd:PRK05249 255 SGKKIKADCLLYANGRTGNTDglnLE-NAGLEADsRGqLKVNENYQTAVPHIYAVGD 310
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
147-227 |
2.33e-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: 59.14 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 147 RVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQVMPGlLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSD 226
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPG-FDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
.
gi 15600542 227 G 227
Cdd:pfam00070 80 G 80
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
146-319 |
2.80e-10 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 61.76 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 146 RRVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQVMPGLLHPAAAkAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLS 225
Cdd:PLN02507 204 KRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRA-VVARNLEGRGINLHPRTNLTQLTKTEGGIKVITD 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 226 DGEVIPCDLVVSAVGLRPRTE-LAF-AAGLAVNR--GIVVDRSLRTSHANIYALGDCAevDGLNLLYVmPLMAcARALAQ 301
Cdd:PLN02507 283 HGEEFVADVVLFATGRAPNTKrLNLeAVGVELDKagAVKVDEYSRTNIPSIWAIGDVT--NRINLTPV-ALME-GTCFAK 358
|
170
....*....|....*....
gi 15600542 302 T-LAGNPSQVAYGPMPVTV 319
Cdd:PLN02507 359 TvFGGQPTKPDYENVACAV 377
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
96-316 |
3.44e-10 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 61.48 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 96 GEEEVRYRDLVLAWGAEPIR---VPVEGDAqdalypINDLEDYARFRQAAAgkrRVLLLGAGLIGCEFANDLSSGGYQLD 172
Cdd:PRK06327 140 DETVITAKHVIIATGSEPRHlpgVPFDNKI------ILDNTGALNFTEVPK---KLAVIGAGVIGLELGSVWRRLGAEVT 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 173 VVapceQVMPGLLhPAA----AKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDG----EVIPCDLVVSAVGLRPR 244
Cdd:PRK06327 211 IL----EALPAFL-AAAdeqvAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDAdgeaQTLEVDKLIVSIGRVPN 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 245 TE--LAFAAGLAVN-RG-IVVDRSLRTSHANIYALGDC---------AEVDGLnllyvmplmacarALAQTLAGNPSQVA 311
Cdd:PRK06327 286 TDglGLEAVGLKLDeRGfIPVDDHCRTNVPNVYAIGDVvrgpmlahkAEEEGV-------------AVAERIAGQKGHID 352
|
....*
gi 15600542 312 YGPMP 316
Cdd:PRK06327 353 YNTIP 357
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
152-281 |
1.55e-09 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 59.10 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 152 GAGLIGCEFANDLSSGGYQLDVVAPCEQVMPGLlHPAAAKAVQAGLEGLGVRfhlgpVL-----ASLKKAGEGLEAHLSD 226
Cdd:PRK07845 184 GSGVTGAEFASAYTELGVKVTLVSSRDRVLPGE-DADAAEVLEEVFARRGMT-----VLkrsraESVERTGDGVVVTLTD 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 227 GEVIPCDLVVSAVGLRPRTE---LAfAAGLAVNRG--IVVDRSLRTSHANIYALGDCAEV 281
Cdd:PRK07845 258 GRTVEGSHALMAVGSVPNTAglgLE-EAGVELTPSghITVDRVSRTSVPGIYAAGDCTGV 316
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
3-308 |
1.77e-09 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 59.01 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 3 ERAPLVIIGTGLAGYNLARewrKLDGE---------------TPLLmitaddgrsyskPMLSTGFSKNKdadglAMAEPG 67
Cdd:PTZ00318 9 KKPNVVVLGTGWAGAYFVR---NLDPKkynitvisprnhmlfTPLL------------PQTTTGTLEFR-----SICEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 68 AMAEQLNARILTHTRVTGIDPGHQRIWIGEE-----------EVRYRDLVLAWGAEPIRVPVEGdAQDALYPINDLEDYA 136
Cdd:PTZ00318 69 RPALAKLPNRYLRAVVYDVDFEEKRVKCGVVsksnnanvntfSVPYDKLVVAHGARPNTFNIPG-VEERAFFLKEVNHAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 137 RFRQ--------------AAAGKRRVL---LLGAGLIGCEFANDLSSGgYQLDVvapcEQVMPGLLHPAAAKAVQAGLEG 199
Cdd:PTZ00318 148 GIRKrivqcieraslpttSVEERKRLLhfvVVGGGPTGVEFAAELADF-FRDDV----RNLNPELVEECKVTVLEAGSEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 200 LGV--------------RFHLGPVLASLKKAGEGLEAHLSDGEVIPCDLVV--SAVGLRPRTElAFAAGLAVNRGIVVDR 263
Cdd:PTZ00318 223 LGSfdqalrkygqrrlrRLGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVwsTGVGPGPLTK-QLKVDKTSRGRISVDD 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15600542 264 SLRTSHA-NIYALGDCAEVDGLNLlyvmPLMA---------CARALAQTLAGNPS 308
Cdd:PTZ00318 302 HLRVKPIpNVFALGDCAANEERPL----PTLAqvasqqgvyLAKEFNNELKGKPM 352
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
62-277 |
7.42e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 53.98 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 62 AMAEPGAMAEQLNAR---ILTHTRVTGIDpGHQR--------IWIGEE--EVRYRDLVLAWGAEPIRVPVEGDAQDAlyp 128
Cdd:PRK07251 67 VMATKNTVTSRLRGKnyaMLAGSGVDLYD-AEAHfvsnkvieVQAGDEkiELTAETIVINTGAVSNVLPIPGLADSK--- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 129 inDLEDYARFRQAAAGKRRVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQVMPgLLHPAAAKAVQAGLEGLGVRFHLGP 208
Cdd:PRK07251 143 --HVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP-REEPSVAALAKQYMEEDGITFLLNA 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600542 209 VLASLKKAGEGLeAHLSDGEVIPCDLVVSAVGLRPRTE---LAFAAGLAVNRG-IVVDRSLRTSHANIYALGD 277
Cdd:PRK07251 220 HTTEVKNDGDQV-LVVTEDETYRFDALLYATGRKPNTEplgLENTDIELTERGaIKVDDYCQTSVPGVFAVGD 291
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
96-289 |
1.19e-07 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 53.48 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 96 GEEEVRYRDLVLAWGAEPIRVPVEGDAQDAlyPINDLEDYARFRQAAAgkrRVLLLGAGLIGCEFANDLSSGGYQLDVVA 175
Cdd:PRK08010 114 GNLEIHGEKIFINTGAQTVVPPIPGITTTP--GVYDSTGLLNLKELPG---HLGILGGGYIGVEFASMFANFGSKVTILE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 176 PCEQVMPgLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIpCDLVVSAVGLRPRTELAFA--AGL 253
Cdd:PRK08010 189 AASLFLP-REDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLA-VDALLIASGRQPATASLHPenAGI 266
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600542 254 AVNR--GIVVDRSLRTSHANIYALGDCaeVDGLNLLYV 289
Cdd:PRK08010 267 AVNErgAIVVDKYLHTTADNIWAMGDV--TGGLQFTYI 302
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
97-322 |
6.59e-07 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 50.98 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 97 EEEVRYRDLVLAWGAEP-IRVPVEGDAQdalYPINdlEDYARFRQAAAGKrrVLLLGAGLIGCEFANDLSSGGYQLdVVA 175
Cdd:PTZ00052 140 EETITAKYILIATGGRPsIPEDVPGAKE---YSIT--SDDIFSLSKDPGK--TLIVGASYIGLETAGFLNELGFDV-TVA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 176 PCEQVMPGLLHPAAAKaVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIPCDLVVSAVGLRPRTelafaAGLAV 255
Cdd:PTZ00052 212 VRSIPLRGFDRQCSEK-VVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDI-----KGLNL 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600542 256 NR-GIVVDRSLR-------TSHANIYALGDCAEvdglNLLYVMPLMACA-RALAQTLAGNPSQVA-YGPMPVTVKTP 322
Cdd:PTZ00052 286 NAiGVHVNKSNKiiapndcTNIPNIFAVGDVVE----GRPELTPVAIKAgILLARRLFKQSNEFIdYTFIPTTIFTP 358
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
228-279 |
8.06e-07 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 50.52 E-value: 8.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600542 228 EVIPCDLVVSAVGLRPRTELAFAA-GLAVNRG--IVVD-RSLRTSHANIYALGDCA 279
Cdd:COG0493 356 FTLPADLVILAIGQTPDPSGLEEElGLELDKRgtIVVDeETYQTSLPGVFAGGDAV 411
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
98-337 |
1.23e-06 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 50.36 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 98 EEVRYRDLVLAWGAEPIRVPVEGD-----AQDALYpindLEDyarfrqaaaGKRRVLLLGAGLIGCEFA---NDLSSGGY 169
Cdd:TIGR01423 148 ERLQAEHILLATGSWPQMLGIPGIehcisSNEAFY----LDE---------PPRRVLTVGGGFISVEFAgifNAYKPRGG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 170 QLDVVAPCEQVMPGL---LHPAAAKAVQAglEGLGVRFHLGPVLASLKKAGEGlEAHLSDGEVIPCDLVVSAVGLRPRTE 246
Cdd:TIGR01423 215 KVTLCYRNNMILRGFdstLRKELTKQLRA--NGINIMTNENPAKVTLNADGSK-HVTFESGKTLDVDVVMMAIGRVPRTQ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 247 L----AFAAGLAVNRGIVVDRSLRTSHANIYALGDcaeVDGLNLLYVMPLMACArALAQTLAGNPSQvaygpmpVTVKTP 322
Cdd:TIGR01423 292 TlqldKVGVELTKKGAIQVDEFSRTNVPNIYAIGD---VTDRVMLTPVAINEGA-AFVDTVFGNKPR-------KTDHTR 360
|
250
....*....|....*
gi 15600542 323 ACPLVVSPPPRGMDG 337
Cdd:TIGR01423 361 VASAVFSIPPIGTCG 375
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
59-278 |
2.79e-06 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 49.38 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 59 DGLAMAEPG----AMAEQLNARI--LTHTRVTGIDPGHQRIWIGEEEVRYRD---LV--LAWGAEPI----RVPVEGDAQ 123
Cdd:PRK13748 164 GGIAATVPTidrsRLLAQQQARVdeLRHAKYEGILDGNPAITVLHGEARFKDdqtLIvrLNDGGERVvafdRCLIATGAS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 124 DALYPINDLED--YARFRQAAAGKR---RVLLLGAGLIGCEFANDLSSGGYQLDVVApceqvMPGLLH---PAAAKAVQA 195
Cdd:PRK13748 244 PAVPPIPGLKEtpYWTSTEALVSDTipeRLAVIGSSVVALELAQAFARLGSKVTILA-----RSTLFFredPAIGEAVTA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 196 GL--EGLGVRFHLGPvlASLKKAGEGLEAHLSDGEVIpCDLVVSAVGLRPRT-ELAF-AAGLAVNRG--IVVDRSLRTSH 269
Cdd:PRK13748 319 AFraEGIEVLEHTQA--SQVAHVDGEFVLTTGHGELR-ADKLLVATGRAPNTrSLALdAAGVTVNAQgaIVIDQGMRTSV 395
|
....*....
gi 15600542 270 ANIYALGDC 278
Cdd:PRK13748 396 PHIYAAGDC 404
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
202-279 |
4.82e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 48.25 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 202 VRFHLGPVLASlkkaGEGLEAHLSDGEVIPCDLVVSAVGLRPRTELAFAA-GLAVNRG---IVVDRSLRTSHANIYALGD 277
Cdd:PRK11749 350 VRMELGEPDAS----GRRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTpGLELNRWgtiIADDETGRTSLPGVFAGGD 425
|
..
gi 15600542 278 CA 279
Cdd:PRK11749 426 IV 427
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
147-322 |
3.66e-05 |
|
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: 45.61 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 147 RVLLLGAGLIGCEFANDLSSGGYQLDVVAPcEQVMPGLLHPAAAKaVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSD 226
Cdd:TIGR01438 182 KTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDCANK-VGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 227 GEVIPC---DLVVSAVGLRPRTE-LAF-AAGLAVNRG---IVVDRSLRTSHANIYALGDCAEvdglNLLYVMPL-MACAR 297
Cdd:TIGR01438 260 STNGIEeeyDTVLLAIGRDACTRkLNLeNVGVKINKKtgkIPADEEEQTNVPYIYAVGDILE----DKPELTPVaIQAGR 335
|
170 180
....*....|....*....|....*.
gi 15600542 298 ALAQTLAGNPSQ-VAYGPMPVTVKTP 322
Cdd:TIGR01438 336 LLAQRLFKGSTViCDYENVPTTVFTP 361
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
146-337 |
3.91e-05 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 45.64 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 146 RRVLLLGAGLIGCEFA---NDLSSggyQLDVVAPCEQVMPGLLHPAAA-KAVQAGLEGlgVRFHLGPVLASLKKAGEG-L 220
Cdd:PLN02546 253 EKIAIVGGGYIALEFAgifNGLKS---DVHVFIRQKKVLRGFDEEVRDfVAEQMSLRG--IEFHTEESPQAIIKSADGsL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600542 221 EAHLSDGEVIPCDLVVSAVGLRPRTELAFAAGLAV----NRGIVVDRSLRTSHANIYALGDCAevDGLNLLYVmPLMAcA 296
Cdd:PLN02546 328 SLKTNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVkmdkNGAIEVDEYSRTSVPSIWAVGDVT--DRINLTPV-ALME-G 403
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600542 297 RALAQTLAGN-PSQVAYGPMPVTvktpacplVVSPPPRGMDG 337
Cdd:PLN02546 404 GALAKTLFGNePTKPDYRAVPSA--------VFSQPPIGQVG 437
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
228-279 |
2.80e-04 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 42.94 E-value: 2.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600542 228 EVIPCDLVVSAVGlrPRTELAF---AAGLAVNRGIV-VDRSLR-TSHANIYALGDCA 279
Cdd:PRK12771 365 ETLEADLVVLAIG--QDIDSAGlesVPGVEVGRGVVqVDPNFMmTGRPGVFAGGDMV 419
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
228-278 |
7.73e-04 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 41.30 E-value: 7.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600542 228 EVIPCDLVVSAVGLRPrTELAFAAGLAV---NRGIVV--DRSLRTSHANIYALGDC 278
Cdd:PRK12810 385 FVLPADLVLLAMGFTG-PEAGLLAQFGVeldERGRVAapDNAYQTSNPKVFAAGDM 439
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
198-242 |
9.47e-04 |
|
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
Pssm-ID: 396255 [Multi-domain] Cd Length: 446 Bit Score: 40.94 E-value: 9.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15600542 198 EGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIPCDLVVSAVGLR 242
Cdd:pfam01593 215 QLLGGDVRLNTRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPLG 259
|
|
| NAD_binding_9 |
pfam13454 |
FAD-NAD(P)-binding; |
185-240 |
2.14e-03 |
|
FAD-NAD(P)-binding;
Pssm-ID: 433222 [Multi-domain] Cd Length: 155 Bit Score: 38.41 E-value: 2.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600542 185 LHPAAAKAVQAGLEGLGVRFHLGPVLaSLKKAGEGLEAHLSDGEVIPCDLVVSAVG 240
Cdd:pfam13454 99 LRDRFEEALARAPAGVTVRVHRARVT-DLRPRGDGYRVLLADGRTLAADAVVLATG 153
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
230-278 |
4.92e-03 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 38.94 E-value: 4.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15600542 230 IPCDLVVSAVGLRPRTELAFAAGLAVNRG--IVVDR-SLRTSHANIYALGDC 278
Cdd:PRK12814 424 LQADTVISAIGQQVDPPIAEAAGIGTSRNgtVKVDPeTLQTSVAGVFAGGDC 475
|
|
| |
