|
Name |
Accession |
Description |
Interval |
E-value |
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
36-416 |
3.77e-150 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 431.48 E-value: 3.77e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 36 ITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVMDIDREAKTITIAElrdekgdllvpERKVPY 115
Cdd:COG1252 30 VTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLAD-----------GRTLSY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 116 DTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANlganGKVNIAIVGGGATGVELSAELHNAVKQ 195
Cdd:COG1252 99 DYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVGGGPTGVELAGELAELLRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 196 LHSYgyKGLTNEALNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIKADLMVWAAG 275
Cdd:COG1252 175 LLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 276 IKAPDFMKEIGgLETNRINQLVVEPTLQTSRDPDIYAIGDCASCARPEGGFVPPRAQAAHQMASCAMNNILAQMNGKPLK 355
Cdd:COG1252 253 VKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIAALLRGKPLK 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901822 356 AYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMVEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252 332 PFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
36-338 |
8.81e-58 |
|
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: 191.76 E-value: 8.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 36 ITLV-DRNHSHLWKPLLHEVATGSLDEGVDAL---SYLAHARNHGFQFQLG-------SVMDIDREAKTITIAELRDEKG 104
Cdd:pfam07992 26 VTLIeDEGTCPYGGCVLSKALLGAAEAPEIASlwaDLYKRKEEVVKKLNNGievllgtEVVSIDPGAKKVVLEELVDGDG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 105 dllvpeRKVPYDTLVMALGSTSNDFNTPGVKENCIFL-DNPHQARRFHQEMLNLflkysanlgangkvNIAIVGGGATGV 183
Cdd:pfam07992 106 ------ETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------------RVVVVGGGYIGV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 184 ELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGG----LHT 259
Cdd:pfam07992 166 ELAAALAKLGKE---------------VTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGdgveVIL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851901822 260 KDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDCascarpeGGFVPPRAQAAHQMA 338
Cdd:pfam07992 231 KDGTEIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTS-VPGIYAAGDC-------RVGGPELAQNAVAQG 301
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
41-401 |
1.19e-44 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 160.70 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 41 RNHsHLWKPLLHEVATGSLdEGVDALSYLAHARNH-GFQFQLGSVMDIDREAKTITIaELRDEKGDLLVPERKVPYDTLV 119
Cdd:PTZ00318 42 RNH-MLFTPLLPQTTTGTL-EFRSICEPVRPALAKlPNRYLRAVVYDVDFEEKRVKC-GVVSKSNNANVNTFSVPYDKLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 120 MALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKysANLG------ANGKVNIAIVGGGATGVELSAELHNAV 193
Cdd:PTZ00318 119 VAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIER--ASLPttsveeRKRLLHFVVVGGGPTGVEFAAELADFF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 194 KQLHSYGYKGLTNEAlNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIKADLMVWA 273
Cdd:PTZ00318 197 RDDVRNLNPELVEEC-KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVWS 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 274 AGIKAPDFMKEIGGLETNRiNQLVVEPTLQTSRDPDIYAIGDCASCarpEGGFVPPRAQAAHQMASCAMNNILAQMNGKP 353
Cdd:PTZ00318 276 TGVGPGPLTKQLKVDKTSR-GRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAKEFNNELKGKP 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 851901822 354 L-KAYQYKDHGSLVSLSNFSTVGSLmgnltrGSMMVEGRIARFVYISLY 401
Cdd:PTZ00318 352 MsKPFVYRSLGSLAYLGNYSAIVQL------GAFDLSGFKALLFWRSAY 394
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
36-355 |
1.75e-38 |
|
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: 141.49 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 36 ITLVDRNHSH------LWKPLLHEVATgsldegVDALSYLAHA--RNHGFQFQLGS-VMDIDREAKTITIAElrdekgdl 106
Cdd:COG0446 8 ITVIEKGPHHsyqpcgLPYYVGGGIKD------PEDLLVRTPEsfERKGIDVRTGTeVTAIDPEAKTVTLRD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 107 lvpERKVPYDTLVMALGSTSNDFNTPGVKENCIF-LDNPHQARRFHQEMLNlflkysanlgANGKvNIAIVGGGATGVEL 185
Cdd:COG0446 74 ---GETLSYDKLVLATGARPRPPPIPGLDLPGVFtLRTLDDADALREALKE----------FKGK-RAVVIGGGPIGLEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 186 SAELHNAvkqlhsygykGLtnealNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGG---LHTKDG 262
Cdd:COG0446 140 AEALRKR----------GL-----KVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDkvaVTLTDG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 263 EYIKADLMVWAAGIkAPDFmkEIG---GLETNRINQLVVEPTLQTSrDPDIYAIGDCASCARPEGG--FVPPRAQAAHQM 337
Cdd:COG0446 205 EEIPADLVVVAPGV-RPNT--ELAkdaGLALGERGWIKVDETLQTS-DPDVYAAGDCAEVPHPVTGktVYIPLASAANKQ 280
|
330
....*....|....*...
gi 851901822 338 ASCAMNNILaqmnGKPLK 355
Cdd:COG0446 281 GRVAAENIL----GGPAP 294
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
48-346 |
1.47e-36 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 138.35 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 48 KPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGS-VMDIDREAKTITiaelrDEKGdllvpeRKVPYDTLVMALGSTS 126
Cdd:COG1251 42 RPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTrVTAIDRAARTVT-----LADG------ETLPYDKLVLATGSRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 127 NDFNTPGV-KENCIFLDNPHQARRFHQEMlnlflkysanlgANGKvNIAIVGGGATGVELSAELHNAvkqlhsyGYKglt 205
Cdd:COG1251 111 RVPPIPGAdLPGVFTLRTLDDADALRAAL------------APGK-RVVVIGGGLIGLEAAAALRKR-------GLE--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 206 nealnVTLVEAGERILP-ALPPRISSAAHNELTKLGVRVLTQTMVTS--ADEG--GLHTKDGEYIKADLMVWAAGIKaP- 279
Cdd:COG1251 168 -----VTVVERAPRLLPrQLDEEAGALLQRLLEALGVEVRLGTGVTEieGDDRvtGVRLADGEELPADLVVVAIGVR-Pn 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 280 -DFMKEIGgLETNR-InqlVVEPTLQTSrDPDIYAIGDCASCA-RPEGGFVPPRAQAAHQMASCAMNNIL 346
Cdd:COG1251 242 tELARAAG-LAVDRgI---VVDDYLRTS-DPDIYAAGDCAEHPgPVYGRRVLELVAPAYEQARVAAANLA 306
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
84-348 |
2.53e-22 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 97.68 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 84 VMDIDREAKTITiaelrdekgdllVPERKVPYDTLVMALGSTSndFNTPGVKENCIFLDNPHQARRFHQEMLnlflkysa 163
Cdd:PRK04965 81 VTDIDAEAQVVK------------SQGNQWQYDKLVLATGASA--FVPPIPGRELMLTLNSQQEYRAAETQL-------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 164 nlgANGKvNIAIVGGGATGVELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPAL-PPRISSAAHNELTKLGVR 242
Cdd:PRK04965 139 ---RDAQ-RVLVVGGGLIGTELAMDLCRAGKA---------------VTLVDNAASLLASLmPPEVSSRLQHRLTEMGVH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 243 VLTQTMVTSAD--EGGLH--TKDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRinQLVVEPTLQTSrDPDIYAIGDCAS 318
Cdd:PRK04965 200 LLLKSQLQGLEktDSGIRatLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNR--GIVVDSYLQTS-APDIYALGDCAE 276
|
250 260 270
....*....|....*....|....*....|
gi 851901822 319 CarpeGGFVPPRAQAAHQMASCAMNNILAQ 348
Cdd:PRK04965 277 I----NGQVLPFLQPIQLSAMALAKNLLGQ 302
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
173-359 |
2.02e-21 |
|
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: 95.92 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVEL-SAelhnavkqLHSYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTS 251
Cdd:COG1249 171 LVVIGGGYIGLEFaQI--------FARLGSE--------VTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 252 ADEGG----LHTKDG---EYIKADLMVWAAGIKApdFMKEIG----GLETNRINQLVVEPTLQTSrDPDIYAIGDCAsca 320
Cdd:COG1249 235 VEKTGdgvtVTLEDGggeEAVEADKVLVATGRRP--NTDGLGleaaGVELDERGGIKVDEYLRTS-VPGIYAIGDVT--- 308
|
170 180 190
....*....|....*....|....*....|....*....
gi 851901822 321 rpeGGfvPPRAQAAHQMASCAMNNILaqmnGKPLKAYQY 359
Cdd:COG1249 309 ---GG--PQLAHVASAEGRVAAENIL----GKKPRPVDY 338
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
50-361 |
7.66e-21 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 95.28 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 50 LLHEVATGSLDEGVDALSYLAHARNHGFQFQLG-SVMDIDREAKTITIAElrdekgdllvpERKVPYDTLVMALGSTSND 128
Cdd:TIGR02374 42 LLSSVLQGEADLDDITLNSKDWYEKHGITLYTGeTVIQIDTDQKQVITDA-----------GRTLSYDKLILATGSYPFI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 129 FNTPGV-KENCifldnpHQARRFH--QEMLNlflkysanlGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYK-GL 204
Cdd:TIGR02374 111 LPIPGAdKKGV------YVFRTIEdlDAIMA---------MAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHApGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 205 TNEALNvtlvEAGERILpalpprissaaHNELTKLGVRVLTQT----MVTSADEGGLHTKDGEYIKADLMVWAAGIKAPD 280
Cdd:TIGR02374 176 MAKQLD----QTAGRLL-----------QRELEQKGLTFLLEKdtveIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 281 FMKEIGGLETNRinQLVVEPTLQTSrDPDIYAIGDCASCARPEGGFVPPraqaAHQMASCAMNNILaqmnGKPLKAYQYK 360
Cdd:TIGR02374 241 ELAVSAGIKVNR--GIIVNDSMQTS-DPDIYAVGECAEHNGRVYGLVAP----LYEQAKVLADHIC----GVECEEYEGS 309
|
.
gi 851901822 361 D 361
Cdd:TIGR02374 310 D 310
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
172-360 |
3.27e-18 |
|
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: 86.54 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 172 NIAIVGGGATGVELSAelhnavkQLHSYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVT- 250
Cdd:TIGR01350 172 SLVIIGGGVIGIEFAS-------IFASLGSK--------VTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTa 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 251 -SADEGGLHTK----DGEYIKADLMVWAAGIKaPDFmKEIG----GLETNRINQLVVEPTLQTSrDPDIYAIGDCAscar 321
Cdd:TIGR01350 237 vEKNDDQVTYEnkggETETLTGEKVLVAVGRK-PNT-EGLGleklGVELDERGRIVVDEYMRTN-VPGIYAIGDVI---- 309
|
170 180 190
....*....|....*....|....*....|....*....
gi 851901822 322 peGGfvPPRAQAAHQMASCAMNNILaqmnGKPLKAYQYK 360
Cdd:TIGR01350 310 --GG--PMLAHVASHEGIVAAENIA----GKEPAHIDYD 340
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
84-318 |
3.41e-16 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 80.08 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 84 VMDIDREAKTITIAELRDEKgdllvpERKVPYDTLVMALGSTSNdfnTPGVKEncIFLDNPHQARRFH--QEMLNLFLKY 161
Cdd:PRK09564 79 VVKVDAKNKTITVKNLKTGS------IFNDTYDKLMIATGARPI---IPPIKN--INLENVYTLKSMEdgLALKELLKDE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 162 SanlgangKVNIAIVGGGATGVELSAELHNAVKqlhsygykgltnealNVTLVEAGERILP-ALPPRISSAAHNELTKLG 240
Cdd:PRK09564 148 E-------IKNIVIIGAGFIGLEAVEAAKHLGK---------------NVRIIQLEDRILPdSFDKEITDVMEEELRENG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 241 VRVLTQTMVTSAD-EG---GLHTKDGEYiKADLMVWAAGIK-APDFMKEiGGLETNRINQLVVEPTLQTSrDPDIYAIGD 315
Cdd:PRK09564 206 VELHLNEFVKSLIgEDkveGVVTDKGEY-EADVVIVATGVKpNTEFLED-TGLKTLKNGAIIVDEYGETS-IENIYAAGD 282
|
...
gi 851901822 316 CAS 318
Cdd:PRK09564 283 CAT 285
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
173-315 |
3.21e-14 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 74.03 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVEL-SAelhnavkqlhsygYKGLTNEalnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTS 251
Cdd:PRK06416 175 LVVIGGGYIGVEFaSA-------------YASLGAE---VTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKK 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851901822 252 ADEGG----LHTKDG---EYIKADLMVWAAGIkAPDfMKEIG----GLETNRiNQLVVEPTLQTSrDPDIYAIGD 315
Cdd:PRK06416 239 VEQTDdgvtVTLEDGgkeETLEADYVLVAVGR-RPN-TENLGleelGVKTDR-GFIEVDEQLRTN-VPNIYAIGD 309
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
173-316 |
1.57e-12 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 69.05 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVEL-SAelhnavkqLHSYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKlGVRVLTQTMVTS 251
Cdd:PRK06292 172 LAVIGGGVIGLELgQA--------LSRLGVK--------VTVFERGDRILPLEDPEVSKQAQKILSK-EFKIKLGAKVTS 234
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901822 252 ADEGG-----LHTKDGE--YIKADLMVWAAGIKA--PDFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDC 316
Cdd:PRK06292 235 VEKSGdekveELEKGGKteTIEADYVLVATGRRPntDGLGLENTGIELDERGRPVVDEHTQTS-VPGIYAAGDV 307
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
75-350 |
3.80e-12 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 68.22 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 75 HGFQFQLGS-VMDIDREAKTItiaelRDEKGdllvpeRKVPYDTLVMALGSTSNdfnTPGVKenciflDNPHQARRFHQE 153
Cdd:PRK14989 72 HGIKVLVGErAITINRQEKVI-----HSSAG------RTVFYDKLIMATGSYPW---IPPIK------GSETQDCFVYRT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 154 MLNL-FLKYSANLGANGkvniAIVGGGATGVELSAelhnAVKQLhsygykGLTNEALNVTLVEAGERilpaLPPRISSAA 232
Cdd:PRK14989 132 IEDLnAIEACARRSKRG----AVVGGGLLGLEAAG----ALKNL------GVETHVIEFAPMLMAEQ----LDQMGGEQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 233 HNELTKLGVRVLT----QTMVTSADEGG--LHTKDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRINQLVVEPTLQTSr 306
Cdd:PRK14989 194 RRKIESMGVRVHTskntLEIVQEGVEARktMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTS- 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 851901822 307 DPDIYAIGDCASCARPEGGFVPPraqaAHQMASCAMNNILAQMN 350
Cdd:PRK14989 273 DPDIYAIGECASWNNRVFGLVAP----GYKMAQVAVDHLLGSEN 312
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
172-256 |
1.09e-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: 60.30 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 172 NIAIVGGGATGVELSAELHNavkqlhsYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTS 251
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALAR-------LGSK--------VTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEA 65
|
....*
gi 851901822 252 ADEGG 256
Cdd:pfam00070 66 IEGNG 70
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
99-324 |
3.06e-11 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 64.56 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 99 LRDEKGDLLVPERKVPYDTLVMALGSTSNDFNT-PGVKENCIFLDNPHQARRFHQEMlnlflkysanlgANGKvNIAIVG 177
Cdd:PRK09754 85 GRDTRELVLTNGESWHWDQLFIATGAAARPLPLlDALGERCFTLRHAGDAARLREVL------------QPER-SVVIVG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 178 GGATGVELSAElhnavkqlhsygykgLTNEALNVTLVEAGERIL-PALPPRISSAAHNELTKLGVRVLTQTMVTSADEGG 256
Cdd:PRK09754 152 AGTIGLELAAS---------------ATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901822 257 ---LHTKDGEYIKADLMVWAAGIKAPDFMKEIGGLETNriNQLVVEPTLQTSrDPDIYAIGDCASCARPEG 324
Cdd:PRK09754 217 kveLTLQSGETLQADVVIYGIGISANDQLAREANLDTA--NGIVIDEACRTC-DPAIFAGGDVAITRLDNG 284
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
173-316 |
7.58e-11 |
|
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: 63.60 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSAELHNAvkqlhsygykgltneALNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVT-- 250
Cdd:TIGR02053 169 LAVIGGGAIGVELAQAFARL---------------GSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKav 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901822 251 SADEGG----LHTKDGEY-IKADLMVWAAGiKAPDFMK---EIGGLETNRINQLVVEPTLQTSrDPDIYAIGDC 316
Cdd:TIGR02053 234 SVRGGGkiitVEKPGGQGeVEADELLVATG-RRPNTDGlglEKAGVKLDERGGILVDETLRTS-NPGIYAAGDV 305
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
173-316 |
8.27e-10 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 60.56 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSAELHnavkqlhsygykGLTNEalnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTS- 251
Cdd:PRK06116 170 VAVVGAGYIAVEFAGVLN------------GLGSE---THLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAv 234
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 851901822 252 --ADEGGL--HTKDGEYIKADLMVWAAGiKAP---DFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDC 316
Cdd:PRK06116 235 ekNADGSLtlTLEDGETLTVDCLIWAIG-REPntdGLGLENAGVKLNEKGYIIVDEYQNTN-VPGIYAVGDV 304
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
173-353 |
2.14e-09 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 59.01 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVElsaelhnavkqlhsY-------GYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLT 245
Cdd:PRK05249 178 LIIYGAGVIGCE--------------YasifaalGVK--------VTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 246 QTMVTS--ADEGG--LHTKDGEYIKADLMVWAAG-IKAPDFMK-EIGGLETNRINQLVVEPTLQTSRdPDIYAIGDCAsc 319
Cdd:PRK05249 236 NEEVEKveGGDDGviVHLKSGKKIKADCLLYANGrTGNTDGLNlENAGLEADSRGQLKVNENYQTAV-PHIYAVGDVI-- 312
|
170 180 190
....*....|....*....|....*....|....
gi 851901822 320 arpegGFvPPRAQAAHQMASCAMNNILAQMNGKP 353
Cdd:PRK05249 313 -----GF-PSLASASMDQGRIAAQHAVGEATAHL 340
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
73-318 |
3.46e-09 |
|
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: 58.61 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 73 RNHGFQFQLGSVMDidreaKTITIAELRDEkgdllvperkvpYDTLVMALGST-SNDFNTPGvkENcifLDNPHQArrfh 151
Cdd:COG0493 182 EALGVEFRTNVEVG-----KDITLDELLEE------------FDAVFLATGAGkPRDLGIPG--ED---LKGVHSA---- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 152 qemlNLFLKySANLG-------ANGKvNIAIVGGGATGVelsaelhNAVKQLHSYGykgltneALNVTLVE-AGERILPA 223
Cdd:COG0493 236 ----MDFLT-AVNLGeapdtilAVGK-RVVVIGGGNTAM-------DCARTALRLG-------AESVTIVYrRTREEMPA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 224 LPPRISSaAHNEltklGVRVLTQTMVTS--ADEGG----LHT---------KDG-----------EYIKADLMVWAAGIK 277
Cdd:COG0493 296 SKEEVEE-ALEE----GVEFLFLVAPVEiiGDENGrvtgLECvrmelgepdESGrrrpvpiegseFTLPADLVILAIGQT 370
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 851901822 278 A-PDFMKEIGGLETNRINQLVVEP-TLQTSRdPDIYAIGDCAS 318
Cdd:COG0493 371 PdPSGLEEELGLELDKRGTIVVDEeTYQTSL-PGVFAGGDAVR 412
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
173-316 |
2.35e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 52.90 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSaelhnavkqlhsYGYKGLTNEalnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSA 252
Cdd:PRK06370 174 LVIIGGGYIGLEFA------------QMFRRFGSE---VTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRV 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901822 253 ----DEGGLHTK---DGEYIKADLMVWAAGiKAP---DFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDC 316
Cdd:PRK06370 239 erdgDGIAVGLDcngGAPEITGSHILVAVG-RVPntdDLGLEAAGVETDARGYIKVDDQLRTT-NPGIYAAGDC 310
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
70-318 |
1.35e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 46.65 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 70 AHARNHGFQFQLGSVMDIDREAKTITIaelRDEKGDLLVPerkvpyDTLVMALGSTSNDFNTPGVKE-------NCIFLD 142
Cdd:COG0492 65 EQAERFGAEILLEEVTSVDKDDGPFRV---TTDDGTEYEA------KAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 143 NPhqarrfhqemlnlFLKysanlganGKvNIAIVGGGATGVELSAElhnavkqlhsygykgLTNEALNVTLVEAGERIlp 222
Cdd:COG0492 136 GF-------------FFR--------GK-DVVVVGGGDSALEEALY---------------LTKFASKVTLIHRRDEL-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 223 alpprisSAAHNELTKL----GVRVLTQTMVTSAD-EGGL------HTKDGE--YIKADLMVWAAGIKAP-DFMKEIgGL 288
Cdd:COG0492 177 -------RASKILVERLranpKIEVLWNTEVTEIEgDGRVegvtlkNVKTGEekELEVDGVFVAIGLKPNtELLKGL-GL 248
|
250 260 270
....*....|....*....|....*....|
gi 851901822 289 ETNRINQLVVEPTLQTSRdPDIYAIGDCAS 318
Cdd:COG0492 249 ELDEDGYIVVDEDMETSV-PGVFAAGDVRD 277
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
222-316 |
2.02e-05 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 46.68 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 222 PALPPRISSAAHNEltklGVRVLTQTMVTS-ADEGG---LHTKDGEyIKADLMVWAAGiKAPDFMK---EIGGLETNRIN 294
Cdd:PRK13748 310 PAIGEAVTAAFRAE----GIEVLEHTQASQvAHVDGefvLTTGHGE-LRADKLLVATG-RAPNTRSlalDAAGVTVNAQG 383
|
90 100
....*....|....*....|..
gi 851901822 295 QLVVEPTLQTSRdPDIYAIGDC 316
Cdd:PRK13748 384 AIVIDQGMRTSV-PHIYAAGDC 404
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
84-318 |
2.34e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 46.31 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 84 VMDIDREAKTITIaelRDEKGDLLVPERkvpYDTLVMalgstsndfnTPGVKENCIFLDNPH--QARRFHQ-EMLNLFLK 160
Cdd:PRK13512 81 VIAINDERQTVTV---LNRKTNEQFEES---YDKLIL----------SPGASANSLGFESDItfTLRNLEDtDAIDQFIK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 161 ysanlgANGKVNIAIVGGGATGVELSAELHNavkqlhsygykgltnEALNVTLVEAGERILPALPPRISSAAHNELTKLG 240
Cdd:PRK13512 145 ------ANQVDKALVVGAGYISLEVLENLYE---------------RGLHPTLIHRSDKINKLMDADMNQPILDELDKRE 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851901822 241 VRVLTQTMVTSADEGGLHTKDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDCAS 318
Cdd:PRK13512 204 IPYRLNEEIDAINGNEVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETN-VPNIYAIGDIIT 280
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
173-316 |
8.73e-04 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 41.52 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSaelhNAVKQLhsygykgltneALNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTM---V 249
Cdd:PTZ00058 240 IGIAGSGYIAVELI----NVVNRL-----------GAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANveeI 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 851901822 250 TSADEGGLHT---KDGEYIKADLMVWAAGiKAPDfMKEIGGLETNRINQ---LVVEPTLQTSRdPDIYAIGDC 316
Cdd:PTZ00058 305 EKVKEKNLTIylsDGRKYEHFDYVIYCVG-RSPN-TEDLNLKALNIKTPkgyIKVDDNQRTSV-KHIYAVGDC 374
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
174-318 |
1.40e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 40.68 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 174 AIVGGGATGVELSAElhnavkqlhsygYKGLTNEalnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSAD 253
Cdd:PRK06327 187 AVIGAGVIGLELGSV------------WRRLGAE---VTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIK 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851901822 254 EGG------LHTKDGEY--IKADLMVWAAGIKA--PDFMKEIGGLETNRINQLVVEPTLQTSRdPDIYAIGDCAS 318
Cdd:PRK06327 252 TGGkgvsvaYTDADGEAqtLEVDKLIVSIGRVPntDGLGLEAVGLKLDERGFIPVDDHCRTNV-PNVYAIGDVVR 325
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
173-315 |
3.54e-03 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 39.61 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSAELHNavkqlhsYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMV--T 250
Cdd:PRK08010 161 LGILGGGYIGVEFASMFAN-------FGSK--------VTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVerI 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851901822 251 SADEGG--LHTKDGEYIkADLMVWAAGIK--APDFMKEIGGLETNRINQLVVEPTLQTSRDpDIYAIGD 315
Cdd:PRK08010 226 SHHENQvqVHSEHAQLA-VDALLIASGRQpaTASLHPENAGIAVNERGAIVVDKYLHTTAD-NIWAMGD 292
|
|
|