|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
43-505 |
0e+00 |
|
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: 587.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAhgKDFASRGIEIPEVRLNLEK 122
Cdd:COG1249 5 DLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEA--RHAAEFGISAGAPSVDWAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 123 MMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKadgsTQVIDTKNILVATGSEVTPFPGITIDEDTIVS 202
Cdd:COG1249 82 LMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGLDEVRVLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 203 STGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNTKVTGAT 282
Cdd:COG1249 158 SDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKVTSVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 283 KKSDGkidVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPML 362
Cdd:COG1249 237 KTGDG---VTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 363 AHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMVKI 441
Cdd:COG1249 314 AHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572640 442 LGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREAnLAAAFGK 505
Cdd:COG1249 394 IADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA-ALALLGR 456
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
43-508 |
0e+00 |
|
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: 568.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-MAHGKDFasrGIEIPEVRLNLE 121
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDeIKHAKDL---GIEVENVSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 122 KMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGsTQVIDTKNILVATGSEVTPFPG-ITIDEDTI 200
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENG-EETLEAKNIIIATGSRPRSLPGpFDFDGKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 201 VSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNTKVTG 280
Cdd:TIGR01350 158 ITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 281 ATKKSDGkidVSVEAaSGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGP 360
Cdd:TIGR01350 237 VEKNDDQ---VTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 361 MLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMV 439
Cdd:TIGR01350 313 MLAHVASHEGIVAAENIAGKEpAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118572640 440 KILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREAnLAAAFGKPIN 508
Cdd:TIGR01350 393 KIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEA-ALAALGKPIH 460
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
43-509 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 568.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIE--KNET----LGGTCLNVGCIPSKALLNNSHYYHMAhGKDFASRGIEIPEV 116
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKgkpaLGGTCLNVGCIPSKALLASSEEFENA-GHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 117 RLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGK----NQVTATKADGSTqvIDTKNILVATGSEVTPFPG 192
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKtdagYEIKVTGEDETV--ITAKHVIIATGSEPRHLPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 193 ITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQRQ 268
Cdd:PRK06327 163 VPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEalpaFLAAA-----DEQVAKEAAKAFTKQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 269 GFKFKLNTKVtGATKKSDGKIDVSVEAASGgKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIP 348
Cdd:PRK06327 238 GLDIHLGVKI-GEIKTGGKGVSVAYTDADG-EAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 349 NIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSR 428
Cdd:PRK06327 316 NVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 429 AKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAfGKPIN 508
Cdd:PRK06327 396 ALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVD-KRPLH 474
|
.
gi 118572640 509 F 509
Cdd:PRK06327 475 F 475
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
38-509 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 546.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 38 QPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-MAHGKDFasrGIEIPEV 116
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADeARHSEDF---GIKAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 117 RLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGsTQVIDTKNILVATGSEVTPFPGITID 196
Cdd:PRK06416 77 GIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELPGIEID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 197 EDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNT 276
Cdd:PRK06416 156 GRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILP-GEDKEISKLAERALKKRGIKIKTGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 277 KVTGATKKSDGkidVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDpKGRIPVNNRFQTKIPNIYAIGDV 356
Cdd:PRK06416 235 KAKKVEQTDDG---VTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 357 VAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTD 436
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572640 437 GMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAfGKPINF 509
Cdd:PRK06416 391 GFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAA-GKPLHA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
40-503 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 531.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 40 IEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAhgKDFASRGIEIPEVRLN 119
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEA--KHAEEFGIHADGPKID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 120 LEKMMEQKHSAVKALTGGIAH-LFKQNKVVHVNGFGKITGKNQVTAtkadgSTQVIDTKNILVATGSEVTPFPGIT-IDE 197
Cdd:PRK06292 79 FKKVMARVRRERDRFVGGVVEgLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPGVWlILG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 198 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQgFKFKLNTK 277
Cdd:PRK06292 154 DRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 278 VTGATKKSDGKIdvsVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVV 357
Cdd:PRK06292 232 VTSVEKSGDEKV---EELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 358 AGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTD 436
Cdd:PRK06292 309 GKPPLLHEAADEGRIAAENAAGDvAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKND 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118572640 437 GMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAF 503
Cdd:PRK06292 389 GFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFS 455
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
38-501 |
2.40e-104 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 319.79 E-value: 2.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 38 QPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKAL---------LNNSHYYHMAHGKdfas 108
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALreavlrligFNQNPLYSSYRVK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 109 RGIEIPEVRLNLEKMMEQKHSAvkaltggIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEvt 188
Cdd:PRK05249 78 LRITFADLLARADHVINKQVEV-------RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 189 PF--PGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE-------FLghvggigiDMEISK 259
Cdd:PRK05249 149 PYrpPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINtrdrllsFL--------DDEISD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 260 NFQRILQRQGFKFKLNTKVTGATKKSDGKIdvsVEAASGGKaevITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPV 339
Cdd:PRK05249 221 ALSYHLRDSGVTIRHNEEVEKVEGGDDGVI---VHLKSGKK---IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 340 NNRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIG 419
Cdd:PRK05249 295 NENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 420 KFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANL 499
Cdd:PRK05249 375 RARFKELARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAAL 454
|
..
gi 118572640 500 AA 501
Cdd:PRK05249 455 DG 456
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
43-503 |
3.79e-104 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 319.46 E-value: 3.79e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMA-HGKDFasrGIEIP-EVRLNL 120
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLArRAAEY---GVSVGgPVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 121 EKMMEQKHSAVKALTGGIAHLFKQNKVVHV-NGFGKITGKNQVtatKADGSTqvIDTKNILVATGSE--VTPFPGItiDE 197
Cdd:PRK06370 83 KAVMARKRRIRARSRHGSEQWLRGLEGVDVfRGHARFESPNTV---RVGGET--LRAKRIFINTGARaaIPPIPGL--DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 198 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNTK 277
Cdd:PRK06370 156 VGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP-REDEDVAAAVREILEREGIDVRLNAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 278 VTGATKKSDGKIdvsVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVV 357
Cdd:PRK06370 235 CIRVERDGDGIA---VGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 358 AGPMLAHKAEDEGIICVEGMA-GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTD 436
Cdd:PRK06370 312 GRGAFTHTAYNDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQ 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118572640 437 GMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFReaNLAAAF 503
Cdd:PRK06370 392 GFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP--TLAQAL 456
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
43-500 |
5.13e-101 |
|
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: 311.66 E-value: 5.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHMAHGkdfASRGIEIPEVRLNLEK 122
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERG-PLGGTCVNVGCVPSKMLLRAAEVAHYARK---PPFGGLAATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 123 MMEQKHSAVKAL-TGGIAHLFKQNKVVHVNGFGKITGKNQVtatKADGSTQVIDTKNILVATGSE--VTPFPGItiDEDT 199
Cdd:TIGR02053 78 LLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTV---KVDLGREVRGAKRFLIATGARpaIPPIPGL--KEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 200 IVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggigIDMEISKNFQRILQRQGFKFKLN 275
Cdd:TIGR02053 153 YLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQrsdrLLPR-----EEPEISAAVEEALAEEGIEVVTS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 276 TKVTGATKKSDGKIDVSVEAASGGKAEVitcDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGD 355
Cdd:TIGR02053 228 AQVKAVSVRGGGKIITVEKPGGQGEVEA---DELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 356 VVAGPMLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNAD 434
Cdd:TIGR02053 305 VTGGLQLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRD 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118572640 435 TDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLA 500
Cdd:TIGR02053 385 TRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQT 450
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
43-494 |
1.00e-78 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 253.16 E-value: 1.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMAH--GKDFasrGIEIPEVRLNL 120
Cdd:PRK06116 6 DLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHdyAPGY---GFDVTENKFDW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 121 EKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVtatKADGstQVIDTKNILVATGSEVTP--FPGItidED 198
Cdd:PRK06116 82 AKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNG--ERYTADHILIATGGRPSIpdIPGA---EY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 199 TIvSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAV----EFLGhvggiGIDMEISKNFQRILQRQGFKFKL 274
Cdd:PRK06116 154 GI-TSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPLR-----GFDPDIRETLVEEMEKKGIRLHT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 275 NTKVTGATKKSDGKIDVSVEaasggKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIG 354
Cdd:PRK06116 228 NAVPKAVEKNADGSLTLTLE-----DGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 355 DVVAGPMLAHKAEDEGIICVEGMAGG--AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEF--KIGKFPFAANSRAK 430
Cdd:PRK06116 303 DVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnvKVYRSSFTPMYTAL 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572640 431 TNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PRK06116 383 TGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
41-502 |
1.02e-72 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 243.28 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 41 EADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNE-TLGGTCLNVGCIPSKALL----------NNSHYYHMAHGKDFASR 109
Cdd:PTZ00153 116 EYDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdSIGGTCVNVGCIPSKALLyatgkyrelkNLAKLYTYGIYTNAFKN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 110 GIEIP---------EVRLNLEKMMEQKHSAVKALTGGIAHLFKQNK-------VVHVNGFGKITGKNQVtatKADGSTQV 173
Cdd:PTZ00153 196 GKNDPvernqlvadTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehVQVIYERGHIVDKNTI---KSEKSGKE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 174 IDTKNILVATGSevTPF--PGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGi 251
Cdd:PTZ00153 273 FKVKNIIIATGS--TPNipDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 252 GIDMEISKNFQRI-LQRQGFKFKLNTKVT-------------GATKKSDGKIDVSVEAASGGKAevITCDVLLVCIGRRP 317
Cdd:PTZ00153 350 LLDADVAKYFERVfLKSKPVRVHLNTLIEyvragkgnqpviiGHSERQTGESDGPKKNMNDIKE--TYVDSCLVATGRKP 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 318 FTQNLGLEELGIELDpKGRIPVNNRFQTK------IPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-------- 383
Cdd:PTZ00153 428 NTNNLGLDKLKIQMK-RGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninven 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 384 -----IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFP--FAANSRA----------------------KTNAD 434
Cdd:PTZ00153 507 waskpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpnnsknnsynkgkyNTVDN 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572640 435 TDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAA 502
Cdd:PTZ00153 587 TEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIA 654
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
43-370 |
6.36e-71 |
|
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: 228.36 E-value: 6.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEknetLGGTCLNVGCIPSKALLNnshyyhmahgkdfasrGIEIPEVRLNLEK 122
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLG----------------AAEAPEIASLWAD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 123 MMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVtatkaDGSTQVIDTKNILVATGSE--VTPFPGIT---IDE 197
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARprLPPIPGVElnvGFL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 198 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNTK 277
Cdd:pfam07992 137 VRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 278 VTGATKKSDGkidVSVEAASGgkaEVITCDVLLVCIGRRPFTQnlGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDV- 356
Cdd:pfam07992 216 VKEIIGDGDG---VEVILKDG---TEIDADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCr 287
|
330
....*....|....
gi 118572640 357 VAGPMLAHKAEDEG 370
Cdd:pfam07992 288 VGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
44-481 |
3.17e-69 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 231.58 E-value: 3.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 44 VTVIGSGPGGYVAAIKSAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASrGIEIPEVRLNLEKM 123
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERG-TIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDG-GIAATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 124 MEQKHSAVKALTG----GIAHLFKQNKVVHvnGFGKITGKNQVTATKADGSTQVIDTKNILVATGSE--VTPFPGITidE 197
Cdd:PRK13748 179 LAQQQARVDELRHakyeGILDGNPAITVLH--GEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASpaVPPIPGLK--E 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 198 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTaveflghvggigidmeisknfqrILQRQGFKFK---- 273
Cdd:PRK13748 255 TPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVT-----------------------ILARSTLFFRedpa 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 274 LNTKVTGATKKSDGKI----DVSVEAASGGKAEVIT------CDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRF 343
Cdd:PRK13748 312 IGEAVTAAFRAEGIEVlehtQASQVAHVDGEFVLTTghgelrADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGM 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 344 QTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPF 423
Cdd:PRK13748 392 RTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTL 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 118572640 424 AANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIA 481
Cdd:PRK13748 472 DNVPRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELA 529
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
46-496 |
3.78e-67 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 222.73 E-value: 3.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 46 VIGSGPGGYVAAIKSAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALLNNSHYYHmahgkDFASrgieipevrlnlekMM 124
Cdd:NF040477 8 IIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQ-----DFST--------------AM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 125 EQKHSAVKALTGGIAH-LFKQNKVVHVNGFGKITGKNQVTATKADGsTQVIDTKNILVATGSEVT--PFPGITIDEDtIV 201
Cdd:NF040477 69 QRKSSVVGFLRDKNYHnLADLDNVDVINGRAEFIDNHTLRVFQADG-EQELRGEKIFINTGAQSVlpPIPGLTTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 202 SSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGiDMEISKNFQRILQRQGFKFKLNTKVTGA 281
Cdd:NF040477 147 DSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPRE-DRDIAQAIATILQDQGVELILNAQVQRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 282 TKKSDGkidVSVEAASGgkaeVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPM 361
Cdd:NF040477 226 SSHEGE---VQLETAEG----VLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 362 LAHKAEDEGIICVEGMAG-GAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMV 439
Cdd:NF040477 299 FTYISLDDFRIVRDSLLGeGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 118572640 440 KILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFRE 496
Cdd:NF040477 379 KAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
43-494 |
6.59e-65 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 216.92 E-value: 6.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALLNNshyyhmahgkdfASRGieipevrLNLE 121
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLLVA------------AEKN-------LSFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 122 KMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGkNQVTATKADGSTQVIDTKNILVATG--SEVTPFPGITiDEDT 199
Cdd:PRK07251 66 QVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVS-NKVIEVQAGDEKIELTAETIVINTGavSNVLPIPGLA-DSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 200 IVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQRQGFKFKLN 275
Cdd:PRK07251 144 VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDaastILPRE-----EPSVAALAKQYMEEDGITFLLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 276 TKVTgATKKSDGKIDVSVEAasggkaEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGD 355
Cdd:PRK07251 219 AHTT-EVKNDGDQVLVVTED------ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 356 VVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNA 433
Cdd:PRK07251 292 VNGGPQFTYISLDDFRIVFGYLTGDGsyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNN 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572640 434 DTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PRK07251 372 DLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
41-494 |
5.15e-64 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 214.70 E-value: 5.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 41 EADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMAHgkDFASRGIEI-PEVRLN 119
Cdd:TIGR01421 2 HYDYLVIGGGSGGIASARRAAEHGAKALLVEAKK-LGGTCVNVGCVPKKVMWYASDLAERMH--DAADYGFYQnDENTFN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 120 LEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADgstqvIDTKNILVATGSEVTPFPGITIDEDT 199
Cdd:TIGR01421 79 WPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPENIPGAELG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 200 IvSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADvTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVT 279
Cdd:TIGR01421 154 T-DSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSE-THLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 280 GATKKSDGKIDVSVEAASggkaEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAG 359
Cdd:TIGR01421 232 KVEKTVEGKLVIHFEDGK----SIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 360 PMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQ-LKEEGIE-FKIGKFPFAANSRAKTNADT 435
Cdd:TIGR01421 308 VELTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYAMTSEKQ 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 118572640 436 DGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:TIGR01421 388 KCRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
43-494 |
7.21e-63 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 213.14 E-value: 7.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLG---------FKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGIEI 113
Cdd:PLN02507 27 DLFVIGAGSGGVRAARFSANFGakvgicelpFHPISSESIGGVGGTCVIRGCVPKKILVYGATF--GGEFEDAKNYGWEI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 114 PE-VRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEVTPfPG 192
Cdd:PLN02507 105 NEkVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQR-PN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 193 ITIDEDTIVSSTgALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVeFLGHVGGIGIDMEISKNFQRILQRQGFKF 272
Cdd:PLN02507 184 IPGKELAITSDE-ALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRAVVARNLEGRGINL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 273 KLNTKVTGATKKSDGkIDVSVEaasggKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYA 352
Cdd:PLN02507 262 HPRTNLTQLTKTEGG-IKVITD-----HGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 353 IGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG---IEFKIGKFPFAANSR 428
Cdd:PLN02507 336 IGDVTNRINLTPVALMEGTCFAKTVFGGqPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdILVFTSSFNPMKNTI 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118572640 429 AKTNADTdgMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PLN02507 416 SGRQEKT--VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
43-494 |
1.06e-62 |
|
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: 212.40 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNET--------LGGTCLNVGCIPSKALLNNSHY-YHMAHGKDFASRGIEi 113
Cdd:TIGR01438 4 DLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgIGGTCVNVGCIPKKLMHQAALLgQALKDSRNYGWKVEE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 114 pEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGsEVTPFPGI 193
Cdd:TIGR01438 83 -TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATG-ERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 194 TIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGI---GIDMEISKNFQRILQRQGF 270
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-----VRSIllrGFDQDCANKVGEHMEEHGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 271 KFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVitcDVLLVCIGRRPFTQNLGLEELGIELDPK-GRIPVNNRFQTKIPN 349
Cdd:TIGR01438 236 KFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEY---DTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 350 IYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQ----LKEEGIEFKIGKF-P 422
Cdd:TIGR01438 313 IYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVIcDYENVPTTVFTPLEYGACGLSEEKavekFGEENVEVFHSYFwP 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118572640 423 FAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:TIGR01438 393 LEWTIPSRDNHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVF 464
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
44-497 |
1.94e-59 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 203.17 E-value: 1.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 44 VTVIGSGPGGYVAAIKSAQLGFKTVCIEkNETLGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGIEI---PEVRLNL 120
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE-RDGLGGAAVLTDCVPSKTLIATAEV--RTELRRAAELGIRFiddGEARVDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 121 EKMmeqkHSAVKALT----GGIAHLFKQNKVVHVNGFGKIT----GKNQVTATKADGSTQVIDTKNILVATGSevTP--F 190
Cdd:PRK07845 81 PAV----NARVKALAaaqsADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGA--SPriL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 191 PGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGF 270
Cdd:PRK07845 155 PTAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLP-GEDADAAEVLEEVFARRGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 271 KFKLNTKVTGATKKSDGkidVSVEAASGGKAEVITCdvlLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNI 350
Cdd:PRK07845 234 TVLKRSRAESVERTGDG---VVVTLTDGRTVEGSHA---LMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 351 YAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRA 429
Cdd:PRK07845 308 YAAGDCTGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572640 430 KTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREA 497
Cdd:PRK07845 388 KMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
46-496 |
2.47e-55 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 191.77 E-value: 2.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 46 VIGSGPGGYVAAIKSAQLGFKTVCIEK-NETLGGTCLNVGCIPSKALLNNSHyyhmAHGkDFAsrgieipevrlnleKMM 124
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGGTCINIGCIPTKTLVHDAQ----QHT-DFV--------------RAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 125 EQKHSAVKALTGGIAH-LFKQNKVVHVNGFGKITGKNQVTATKADGStQVIDTKNILVATGSE--VTPFPGITIDEDtIV 201
Cdd:PRK08010 69 QRKNEVVNFLRNKNFHnLADMPNIDVIDGQAEFINNHSLRVHRPEGN-LEIHGEKIFINTGAQtvVPPIPGITTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 202 SSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQRQGFKFKLNTK 277
Cdd:PRK08010 147 DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslFLPRE-----DRDIADNIATILRDQGVDIILNAH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 278 VTGATKKsDGKIDVSVEAASggkaevITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVV 357
Cdd:PRK08010 222 VERISHH-ENQVQVHSEHAQ------LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 358 AGPMLAHKAEDEGIICVEGMAGGAVHI--DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADT 435
Cdd:PRK08010 295 GGLQFTYISLDDYRIVRDELLGEGKRStdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572640 436 DGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFRE 496
Cdd:PRK08010 375 RGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
43-492 |
5.19e-54 |
|
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: 189.03 E-value: 5.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNET---------LGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGIEI 113
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQY--MDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 114 --PEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNK-VVHVNGFGKITGKNQVTATK-ADGSTQV---IDTKNILVATGS- 185
Cdd:TIGR01423 83 drSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsADPKSAVkerLQAEHILLATGSw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 186 -EVTPFPGItideDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSV---WQRLGADVTaVEFLGHVGGIGIDMEISKNF 261
Cdd:TIGR01423 163 pQMLGIPGI----EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVT-LCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 262 QRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEaaSGGKAEVitcDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNN 341
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTLNADGSKHVTFE--SGKTLDV---DVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 342 RFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQL--KEEGIEFKI 418
Cdd:TIGR01423 313 FSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAakKFEKVAVYE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118572640 419 GKF-PFAANSRAKTNADTdgMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSE 492
Cdd:TIGR01423 393 SSFtPLMHNISGSKYKKF--VAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
389-497 |
4.50e-53 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 174.66 E-value: 4.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 389 VPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAA 468
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 118572640 469 LALEYGASCEDIARVCHAHPTLSEAFREA 497
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
43-503 |
3.18e-52 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 183.62 E-value: 3.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGyvaAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHMAHGKDFASR-GI--EIPEVRLn 119
Cdd:PRK07846 3 DLIIIGTGSGN---SILDERFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAADVARTIREAARlGVdaELDGVRW- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 120 lEKMMEQKHSAVKAL-TGGIAHLFKQNKVVHV-NGFGKITGknQVTATKADGStqVIDTKNILVATGSEVTPFPGITIDE 197
Cdd:PRK07846 76 -PDIVSRVFGRIDPIaAGGEEYRGRDTPNIDVyRGHARFIG--PKTLRTGDGE--EITADQVVIAAGSRPVIPPVIADSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 198 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggigIDMEISKNFQRILQRQgFKFK 273
Cdd:PRK07846 151 VRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNrsgrLLRH-----LDDDISERFTELASKR-WDVR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 274 LNTKVTGATKKSDGkidVSVEAASGgkaEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAI 353
Cdd:PRK07846 225 LGRNVVGVSQDGSG---VTLRLDDG---STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 354 GDVVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKT 431
Cdd:PRK07846 299 GDVSSPYQLKHVANHEARVVQHNLLHPDdlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572640 432 NADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH-AHPTLSEAFREANLAAAF 503
Cdd:PRK07846 379 MEDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
43-494 |
2.68e-48 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 173.86 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIE--KNET------LGGTCLNVGCIPSKALlnnsHYY-HMAH--GKDFASRGI 111
Cdd:PTZ00052 7 DLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLM----HYAaNIGSifHHDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 112 EIPEVrLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVtATKADGSTQVIDTKNILVATGSEvtpfP 191
Cdd:PTZ00052 83 KTSSS-FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGR----P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 192 GITID----EDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGI---GIDMEISKNFQRI 264
Cdd:PTZ00052 157 SIPEDvpgaKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVA-----VRSIplrGFDRQCSEKVVEY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 265 LQRQGFKFKlNTKVTGATKKSDGKIDVSVeaaSGGKAEVItcDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRfQ 344
Cdd:PTZ00052 232 MKEQGTLFL-EGVVPINIEKMDDKIKVLF---SDGTTELF--DTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPND-C 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 345 TKIPNIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFP 422
Cdd:PTZ00052 305 TNIPNIFAVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFiDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 423 FAANS------------RAKTNA-DTD----GMVKILGHKSTD-RVLGAHILGPGAGEMVNEAALALEYGASCEDIARVC 484
Cdd:PTZ00052 385 QEFNTleiaavhrekheRARKDEyDFDvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMI 464
|
490
....*....|
gi 118572640 485 HAHPTLSEAF 494
Cdd:PTZ00052 465 GIHPTDAEVF 474
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
43-500 |
3.43e-47 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 169.94 E-value: 3.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGyvaAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHMAHGKDFASR-GI--EIPEVRLN 119
Cdd:TIGR03452 4 DLIIIGTGSGN---SIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAAEVAQSIGESARlGIdaEIDSVRWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 120 --LEKMMEQKhsaVKALTGGIAHLFKQNKVVHVNGF-GKITGKNQVTATKADGSTqvIDTKNILVATGSEVTPFPGITID 196
Cdd:TIGR03452 78 diVSRVFGDR---IDPIAAGGEDYRRGDETPNIDVYdGHARFVGPRTLRTGDGEE--ITGDQIVIAAGSRPYIPPAIADS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 197 EDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAV----EFLGHvggigIDMEISKNFQRILQRQgFKF 272
Cdd:TIGR03452 153 GVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVnrstKLLRH-----LDEDISDRFTEIAKKK-WDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 273 KLNTKVTGATKKSDGkidVSVEAASGgkaEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYA 352
Cdd:TIGR03452 227 RLGRNVTAVEQDGDG---VTLTLDDG---STVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 353 IGDVVAGPMLAHKAEDEGIICVEGMA--GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG--IEFKIGKFPFAANSR 428
Cdd:TIGR03452 301 LGDVSSPYQLKHVANAEARVVKHNLLhpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGhdITVKIQNYGDVAYGW 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572640 429 AKtnADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH-AHPTLSEAFREANLA 500
Cdd:TIGR03452 381 AM--EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLG 451
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
43-494 |
1.13e-45 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 168.13 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGG---------YVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHmahgkDF-ASRG-- 110
Cdd:PLN02546 81 DLFTIGAGSGGvrasrfasnFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSH-----EFeESRGfg 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 111 -IEIPEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTAtkaDGstQVIDTKNILVATGSEvtP 189
Cdd:PLN02546 156 wKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DG--KLYTARNILIAVGGR--P 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 190 F----PGItideDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAveFLGHVGGI-GIDMEISKNFQRI 264
Cdd:PLN02546 229 FipdiPGI----EHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHV--FIRQKKVLrGFDEEVRDFVAEQ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 265 LQRQGFKFKLNTKVTGATKKSDGKIDVSVEAAS-GGKAEVitcdvlLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRF 343
Cdd:PLN02546 303 MSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTvEGFSHV------MFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 344 QTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIgkfp 422
Cdd:PLN02546 377 RTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNePTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDV---- 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118572640 423 FAANSRAkTNADTDGM-----VKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PLN02546 453 FTANFRP-LKATLSGLpdrvfMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF 528
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
21-494 |
1.90e-42 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 159.01 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 21 SHGLQGvSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHM 100
Cdd:PTZ00058 29 YHNLEA-SSAPTHLKKKPRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKIMFNAASIHDI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 101 AHgkDFASRGIEIPEVrLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATK-------------- 166
Cdd:PTZ00058 107 LE--NSRHYGFDTQFS-FNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeadesddd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 167 ----------ADGSTQVIDTKNILVATGSEvTPFPGITIDEDTIvSSTGALSLKKvPEKLVVIGAGVIGVELGSVWQRLG 236
Cdd:PTZ00058 184 evtivsagvsQLDDGQVIEGKNILIAVGNK-PIFPDVKGKEFTI-SSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 237 ADvTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKksDGKIDVSVEAASGGKAEVITCdvLLVCIGRR 316
Cdd:PTZ00058 261 AE-SYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEK--VKEKNLTIYLSDGRKYEHFDY--VIYCVGRS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 317 PFTQNLGLEELGIeLDPKGRIPVNNRFQTKIPNIYAIGDVVAGP---------MLAHKAEDEGIICVEGMAGGAVH---- 383
Cdd:PTZ00058 336 PNTEDLNLKALNI-KTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnLLKLYNEEPYLKKKENTSGESYYnvql 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 384 ----------------------IDYNCVPSVIYTHPEVAWVGKSEEQLKEE-GIE-FKI----------GKFPFAANSRA 429
Cdd:PTZ00058 415 tpvainagrlladrlfgpfsrtTNYKLIPSVIFSHPPIGTIGLSEQEAIDIyGKEnVKIyesrftnlffSVYDMDPAQKE 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118572640 430 KTnadtdgMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PTZ00058 495 KT------YLKLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
159-393 |
1.77e-30 |
|
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: 120.69 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 159 KNQVTATKADGSTQVIDTKN--------ILVATGSE--VTPFPGITIDE-DTIVSSTGALSLKKV-----PEKLVVIGAG 222
Cdd:COG0446 54 RTGTEVTAIDPEAKTVTLRDgetlsydkLVLATGARprPPPIPGLDLPGvFTLRTLDDADALREAlkefkGKRAVVIGGG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 223 VIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNTKVTGAtkksDGKIDVSVEAASGgkaE 302
Cdd:COG0446 134 PIGLELAEALRKRGLKVTLVERAPRLLG-VLDPEMAALLEEELREHGVELRLGETVVAI----DGDDKVAVTLTDG---E 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 303 VITCDVLLVCIGRRPFTQnLgLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVV----------AGPMLAHKAEDEGII 372
Cdd:COG0446 206 EIPADLVVVAPGVRPNTE-L-AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphpvtgktVYIPLASAANKQGRV 283
|
250 260
....*....|....*....|.
gi 118572640 373 CVEGMAGGAvhIDYNCVPSVI 393
Cdd:COG0446 284 AAENILGGP--APFPGLGTFI 302
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
43-361 |
1.15e-25 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 106.74 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNEtLGGTCLNVGCIpskallNNshYYHMAHGKdfasRGIEIpevrlnLEK 122
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEI------EN--YPGFPEGI----SGPEL------AER 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 123 MMEQ-KHSAVKALTGGIAHLFKQNKVVHVNGfgkitgknqvtatkadGSTQVIDTKNILVATGSEVT--PFPGITIDEDT 199
Cdd:COG0492 63 LREQaERFGAEILLEEVTSVDKDDGPFRVTT----------------DDGTEYEAKAVIIATGAGPRklGLPGEEEFEGR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 200 IVSSTGALSLKKVP-EKLVVIGAGVIGVELGSVWQRLGADVTAVeflgHVGGigiDMEISKNFQ-RILQRQGFKFKLNTK 277
Cdd:COG0492 127 GVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLI----HRRD---ELRASKILVeRLRANPKIEVLWNTE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 278 VTGAtkKSDGKID-VSVEAASGGKAEVITCDVLLVCIGRRPftqNLGL-EELGIELDPKGRIPVNNRFQTKIPNIYAIGD 355
Cdd:COG0492 200 VTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLKP---NTELlKGLGLELDEDGYIVVDEDMETSVPGVFAAGD 274
|
....*.
gi 118572640 356 VVAGPM 361
Cdd:COG0492 275 VRDYKY 280
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
146-382 |
2.34e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 99.06 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 146 KVVHVNgfgkiTGKNQVTAtkADGSTQVIDTknILVATGSE--VTPFPGI---------TIDE-DTIVSSTGAlslkkvP 213
Cdd:COG1251 78 RVTAID-----RAARTVTL--ADGETLPYDK--LVLATGSRprVPPIPGAdlpgvftlrTLDDaDALRAALAP------G 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 214 EKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKidvSV 293
Cdd:COG1251 143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVT---GV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 294 EAASGgkaEVITCDVLLVCIGRRPftqNLGL-EELGIELDpkGRIPVNNRFQTKIPNIYAIGDVVA-------GPMLAH- 364
Cdd:COG1251 220 RLADG---EELPADLVVVAIGVRP---NTELaRAAGLAVD--RGIVVDDYLRTSDPDIYAAGDCAEhpgpvygRRVLELv 291
|
250
....*....|....*....
gi 118572640 365 -KAEDEGIICVEGMAGGAV 382
Cdd:COG1251 292 aPAYEQARVAAANLAGGPA 310
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
155-488 |
3.09e-16 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 80.85 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 155 KITGKNQVTATKADGSTQVIDTK--NILVATG--SEVTPFPGITIDE-DTIVSSTGALSLKKVPEK-----LVVIGAGVI 224
Cdd:PRK09564 81 KVDAKNKTITVKNLKTGSIFNDTydKLMIATGarPIIPPIKNINLENvYTLKSMEDGLALKELLKDeeiknIVIIGAGFI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 225 GVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSveaasgGKAEVI 304
Cdd:PRK09564 161 GLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVT------DKGEYE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 305 TcDVLLVCIGRRPFTQnlGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGD-------VVAGPM---LAHKAEDEGIICV 374
Cdd:PRK09564 235 A-DVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 375 EGMAGGAVH----IDYNCVPSVIYthpEVAWVGKSEEQLKEEGIEFKIgKFPFAANSRAKTNADTDGMVKILGHKSTDRV 450
Cdd:PRK09564 312 ENLAGRHVSfkgtLGSACIKVLDL---EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEADTKVI 387
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 118572640 451 LGAHILGP-GAGEMVNEAALALEYGASCEDIARV--CHAHP 488
Cdd:PRK09564 388 LGGQIIGKkGAVLRIDALAVAIYAKLTTQELGMMdfCYAPP 428
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
215-288 |
1.17e-15 |
|
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: 71.85 E-value: 1.17e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572640 215 KLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGK 288
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV 73
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
93-375 |
2.10e-15 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 77.87 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 93 NNSHYY-HMAHGkdFASRGIEIPEVRLNLEKMMEQKHsaVKaltggiahlFKQNKVVHVNgfgkiTGKNQVTAtkADGST 171
Cdd:COG1252 36 NPYHLFqPLLPE--VAAGTLSPDDIAIPLRELLRRAG--VR---------FIQGEVTGID-----PEARTVTL--ADGRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 172 QVIDTknILVATGSeVTPFPGIT-IDEDtivsstgALSLKKVPE---------------------KLVVIGAGVIGVEL- 228
Cdd:COG1252 96 LSYDY--LVIATGS-VTNFFGIPgLAEH-------ALPLKTLEDalalrerllaaferaerrrllTIVVVGGGPTGVELa 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 229 GSVWQRLG------------ADVTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSdgkidvsVEAA 296
Cdd:COG1252 166 GELAELLRkllrypgidpdkVRITLVEAGPRILP-GLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADG-------VTLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 297 SGgkaEVITCDVLLVCIGRR--PFTQNLGLEelgieLDPKGRIPVNNRFQTK-IPNIYAIGDVVAG--------PMLAHK 365
Cdd:COG1252 238 DG---EEIPADTVIWAAGVKapPLLADLGLP-----TDRRGRVLVDPTLQVPgHPNVFAIGDCAAVpdpdgkpvPKTAQA 309
|
330
....*....|
gi 118572640 366 AEDEGIICVE 375
Cdd:COG1252 310 AVQQAKVLAK 319
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
180-355 |
7.34e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 76.11 E-value: 7.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 180 LV-ATGSE--VTPFPGitiDEDTIV--------SSTGALSLKKvpeKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHV 248
Cdd:PRK04965 103 LVlATGASafVPPIPG---RELMLTlnsqqeyrAAETQLRDAQ---RVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 249 GGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGkidVSVEAASGgkaEVITCDVLLVCIGRRPftqNLGL-EEL 327
Cdd:PRK04965 177 LASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG---IRATLDSG---RSIEVDAVIAAAGLRP---NTALaRRA 247
|
170 180
....*....|....*....|....*...
gi 118572640 328 GIELDpKGrIPVNNRFQTKIPNIYAIGD 355
Cdd:PRK04965 248 GLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
196-357 |
1.85e-14 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 75.20 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 196 DEDTIVSSTGALSLKKVPeklvVIGAGVIGVE-LGSVWQRlGADVTAVEFLGHVGGIgIDMEISKNFQRILQRQGFKFKL 274
Cdd:PRK13512 135 DTDAIDQFIKANQVDKAL----VVGAGYISLEvLENLYER-GLHPTLIHRSDKINKL-MDADMNQPILDELDKREIPYRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 275 NTKVTgatkksdgKIDVSVEAASGGKAEviTCDVLLVCIGRRPFTQNLglEELGIELDPKGRIPVNNRFQTKIPNIYAIG 354
Cdd:PRK13512 209 NEEID--------AINGNEVTFKSGKVE--HYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIG 276
|
...
gi 118572640 355 DVV 357
Cdd:PRK13512 277 DII 279
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
298-370 |
1.45e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 68.86 E-value: 1.45e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572640 298 GGKAEVITCDVLLVCIGRRPfTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAEDEG 370
Cdd:PRK12770 267 PGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
155-358 |
5.54e-12 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 68.32 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 155 KITGKNQVTATKAdGSTQVIDTknILVATGSE--VTPFPGI---------TIDE-DTIvsstgaLSLKKVPEKLVVIGAG 222
Cdd:TIGR02374 79 QIDTDQKQVITDA-GRTLSYDK--LILATGSYpfILPIPGAdkkgvyvfrTIEDlDAI------MAMAQRFKKAAVIGGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 223 VIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKksDGKIDvSVEAASGgkaE 302
Cdd:TIGR02374 150 LLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG--ATKAD-RIRFKDG---S 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 118572640 303 VITCDVLLVCIGRRPFTqnlgleELGIE--LDPKGRIPVNNRFQTKIPNIYAIGDVVA 358
Cdd:TIGR02374 224 SLEADLIVMAAGIRPND------ELAVSagIKVNRGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
44-385 |
3.47e-11 |
|
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: 65.16 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 44 VTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTclnvgcipskallnnshyyhMAHGkdfasrgieIPEVRLNlEKM 123
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL--------------------LRYG---------IPEFRLP-KDV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 124 MEQKHSAVKALtgGIAhlFKQNKVVhvngfgkitGKNqVTATKADGstqviDTKNILVATGSEV---TPFPGItiDEDTI 200
Cdd:COG0493 174 LDREIELIEAL--GVE--FRTNVEV---------GKD-ITLDELLE-----EFDAVFLATGAGKprdLGIPGE--DLKGV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 201 VS----------STGALSLKKVPEKLVVIGAG-----VIGVELgsvwqRLGA-DVTAVEFLGHVggigiDM-----EISK 259
Cdd:COG0493 233 HSamdfltavnlGEAPDTILAVGKRVVVIGGGntamdCARTAL-----RLGAeSVTIVYRRTRE-----EMpaskeEVEE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 260 nfqriLQRQGFKFKLNTKVTGATKKSDG--------KIDVSVEAASG--------GKAEVITCDVLLVCIGRRPFTQNLg 323
Cdd:COG0493 303 -----ALEEGVEFLFLVAPVEIIGDENGrvtglecvRMELGEPDESGrrrpvpieGSEFTLPADLVILAIGQTPDPSGL- 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118572640 324 LEELGIELDPKGRIPVN-NRFQTKIPNIYAIGDVVAGPMLAhkaedegiicVEGMAGG---AVHID 385
Cdd:COG0493 377 EEELGLELDKRGTIVVDeETYQTSLPGVFAGGDAVRGPSLV----------VWAIAEGrkaARAID 432
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
179-356 |
5.31e-10 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 61.09 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 179 ILVATGSEVTPFPGI-TIDED--TIVSSTGALSLKKV--PEKLVVI-GAGVIGVELGSVWQRLGADVTAVEFLGHVGGIG 252
Cdd:PRK09754 104 LFIATGAAARPLPLLdALGERcfTLRHAGDAARLREVlqPERSVVIvGAGTIGLELAASATQRRCKVTVIELAATVMGRN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 253 IDMEISKNFQRILQRQGFKFKLNTKVTGATKKSdgkiDVSVEAASGgkaEVITCDVLLVCIGRRpFTQNLGLEElgiELD 332
Cdd:PRK09754 184 APPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE----KVELTLQSG---ETLQADVVIYGIGIS-ANDQLAREA---NLD 252
|
170 180
....*....|....*....|....
gi 118572640 333 PKGRIPVNNRFQTKIPNIYAIGDV 356
Cdd:PRK09754 253 TANGIVIDEACRTCDPAIFAGGDV 276
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
27-368 |
4.67e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 55.54 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 27 VSSVPLRTY---ADQPIEA---DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTclnvgcipskallnnshyyhM 100
Cdd:PRK13984 263 VDNVPVEKYseiLDDEPEKknkKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV--------------------M 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 101 AHGkdfasrgieIPEVRLNLEkMMEQKHSAVKALTGGIaHLfkQNKVVHVNGFGKITGKNQVtatkadgstqvidtknIL 180
Cdd:PRK13984 323 RYG---------IPSYRLPDE-ALDKDIAFIEALGVKI-HL--NTRVGKDIPLEELREKHDA----------------VF 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 181 VATG---SEVTPFPGiTIDEDTIvsstGALSL--------------KKVPEKLVVIGAGVIGVELGSVWQRLG------A 237
Cdd:PRK13984 374 LSTGftlGRSTRIPG-TDHPDVI----QALPLlreirdylrgegpkPKIPRSLVVIGGGNVAMDIARSMARLQkmeygeV 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 238 DVTAV-------EFLGHVGGI------GIDMEISKNFQRIL----QRQGFKFKLNTKVTGATKKSDGKIDVSVEAasggk 300
Cdd:PRK13984 449 NVKVTslertfeEMPADMEEIeegleeGVVIYPGWGPMEVViendKVKGVKFKKCVEVFDEEGRFNPKFDESDQI----- 523
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118572640 301 aeVITCDVLLVCIGRRPFTQNLGlEELGIELD-PKGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAED 368
Cdd:PRK13984 524 --IVEADMVVEAIGQAPDYSYLP-EELKSKLEfVRGRILTNEYGQTSIPWLFAGGDIVHGPDIIHGVAD 589
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
302-377 |
3.05e-07 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 52.86 E-value: 3.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118572640 302 EVITCDVLLVCIGRRPFTQNLgLEELGIELDPKGRIPVN-NRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGM 377
Cdd:PRK12810 385 FVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPdNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
43-78 |
1.93e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 50.23 E-value: 1.93e-06
10 20 30
....*....|....*....|....*....|....*.
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGG 78
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
217-370 |
2.41e-06 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 49.77 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 217 VVIGAGVIGVELGSVWQRLGAD--------------VTAVEFLGHVGGiGIDMEISKNFQRILQRQGFKFKLNTKVTGAT 282
Cdd:PTZ00318 177 VVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLG-SFDQALRKYGQRRLRRLGVDIRTKTAVKEVL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 283 KKSdgkidvsVEAASGgkaEVITCDVLL--VCIGRRPFTQNLGleelgIELDPKGRIPVNNRFQTK-IPNIYAIGDVVAG 359
Cdd:PTZ00318 256 DKE-------VVLKDG---EVIPTGLVVwsTGVGPGPLTKQLK-----VDKTSRGRISVDDHLRVKpIPNVFALGDCAAN 320
|
170
....*....|....*.
gi 118572640 360 -----PMLAHKAEDEG 370
Cdd:PTZ00318 321 eerplPTLAQVASQQG 336
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
43-92 |
3.99e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 49.09 E-value: 3.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNetlGGTCLNVGCIPSKALL 92
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHN---TDTIAELSCNPSIGGI 47
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
31-79 |
4.57e-06 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 49.33 E-value: 4.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 118572640 31 PLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:PRK06134 2 PSAAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
43-79 |
5.20e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 48.76 E-value: 5.20e-06
10 20 30
....*....|....*....|....*....|....*..
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
38-79 |
9.68e-06 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 48.15 E-value: 9.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 118572640 38 QPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
217-355 |
2.06e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 47.42 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 217 VVIGAGVIGVELGSVWQRLGADVTAVEF--------LGHVGG---------IGIDMEISKNFQRILQrQGfkfklntkvT 279
Cdd:PRK14989 149 AVVGGGLLGLEAAGALKNLGVETHVIEFapmlmaeqLDQMGGeqlrrkiesMGVRVHTSKNTLEIVQ-EG---------V 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118572640 280 GATKksdgkidvSVEAASGGKAEVitcDVLLVCIGRRPftQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGD 355
Cdd:PRK14989 219 EARK--------TMRFADGSELEV---DFIVFSTGIRP--QDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
39-184 |
2.23e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 47.16 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 39 PIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGtclnvgcipsKAllnnSHYYHMAHGKDFASRGieipevrl 118
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG----------RA----AQLHKTFPGLDCPQCI-------- 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572640 119 nLEKMME--QKHSAVKALTGgiahlfkqNKVVHVNGFGkitGKNQVTATKADGSTQVIDTKNILVATG 184
Cdd:COG1148 196 -LEPLIAevEANPNITVYTG--------AEVEEVSGYV---GNFTVTIKKGPREEIEIEVGAIVLATG 251
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
40-79 |
3.03e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 46.36 E-value: 3.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 118572640 40 IEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
41-79 |
3.37e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 46.57 E-value: 3.37e-05
10 20 30
....*....|....*....|....*....|....*....
gi 118572640 41 EADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:PRK07843 7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
43-79 |
5.59e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 45.36 E-value: 5.59e-05
10 20 30
....*....|....*....|....*....|....*..
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
39-78 |
6.23e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 45.59 E-value: 6.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 118572640 39 PIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGG 78
Cdd:PRK12839 6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
44-359 |
1.47e-04 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 44.40 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 44 VTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGtcLNVGCIPSkallnnshyYHMAhgKDFASRGIEipevrlNLEKM 123
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPE---------FRLP--KDIVDREVE------RLLKL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 124 -MEQKHSAV--KALTggIAHLFKQNKVVHVNgfgkiTGKNQVTATKADGStqviDTKNILVAtgsevtpfpgitIDEDTI 200
Cdd:PRK11749 204 gVEIRTNTEvgRDIT--LDELRAGYDAVFIG-----TGAGLPRFLGIPGE----NLGGVYSA------------VDFLTR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 201 VSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGA-DVTAVEFLGHVggigiDMEISKNFQRILQRQGFKFKLNTK-- 277
Cdd:PRK11749 261 VNQAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAeSVTIVYRRGRE-----EMPASEEEVEHAKEEGVEFEWLAApv 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 278 -VTGatkksDGKIDVSVEA---------ASG-------GKAEVITCDVLLVCIGRRPFTQNLGLEElGIELDPKG-RIPV 339
Cdd:PRK11749 336 eILG-----DEGRVTGVEFvrmelgepdASGrrrvpieGSEFTLPADLVIKAIGQTPNPLILSTTP-GLELNRWGtIIAD 409
|
330 340
....*....|....*....|
gi 118572640 340 NNRFQTKIPNIYAIGDVVAG 359
Cdd:PRK11749 410 DETGRTSLPGVFAGGDIVTG 429
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
46-80 |
1.50e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 39.82 E-value: 1.50e-04
10 20 30
....*....|....*....|....*....|....*
gi 118572640 46 VIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTC 80
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
41-86 |
1.55e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 44.41 E-value: 1.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 118572640 41 EADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGG-TCLNVGCI 86
Cdd:PRK12835 11 EVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
41-79 |
1.60e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 44.34 E-value: 1.60e-04
10 20 30
....*....|....*....|....*....|....*....
gi 118572640 41 EADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12843 16 EFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
41-79 |
4.47e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 42.82 E-value: 4.47e-04
10 20 30
....*....|....*....|....*....|....*....
gi 118572640 41 EADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12844 6 TYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
43-79 |
8.79e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 41.77 E-value: 8.79e-04
10 20 30
....*....|....*....|....*....|....*..
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGT 79
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
43-77 |
1.44e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 41.03 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|....*
gi 118572640 43 DVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLG 77
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
249-339 |
1.90e-03 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 40.51 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572640 249 GGIgID-MEISKNFQRILQRQGFKFKLNTKVTGATKKSDGkidVSVEAASGgkaeVITCDVLLVCIGrrpftqnLG---- 323
Cdd:COG0579 147 TGI-VDpGALTRALAENAEANGVELLLNTEVTGIEREGDG---WEVTTNGG----TIRARFVINAAG-------LYadrl 211
|
90
....*....|....*.
gi 118572640 324 LEELGIELDPKGrIPV 339
Cdd:COG0579 212 AQMAGIGKDFGI-FPV 226
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
324-378 |
6.46e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 39.34 E-value: 6.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 118572640 324 LEELGIELDPKGRI--PVNNRF--QTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMA 378
Cdd:PRK12769 590 LESHGVTVDKWGRIiaDVESQYryQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
36-70 |
6.86e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 38.73 E-value: 6.86e-03
10 20 30
....*....|....*....|....*....|....*
gi 118572640 36 ADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCI 70
Cdd:PRK07494 2 LMEKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
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