|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
1-439 |
0e+00 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 750.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 1 MKKhIIVVGAVAGGATSASQIRRLDKDSRITVYEKDSFMSFANCGLPYYLGNVIEERDDILSTNPEKFKAYKDIDVKVKH 80
Cdd:PRK13512 1 MPK-IIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFYDRKQITVKTYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 81 EVLKIDDKKQTVTVKNHFTGETFEDAYDALVLSPGARASQLNFDVPHLFTLRNMDDTDQIDTYIRQYNVKTVLIVGAGYV 160
Cdd:PRK13512 80 EVIAINDERQTVTVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDKALVVGAGYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 161 SLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGHTVTFTSGAVEDYDLIIAGVGV 240
Cdd:PRK13512 160 SLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVEHYDMIIEGVGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 241 RPNSEFIQNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSFYRHVDLPAHVPLAWGAHRGASIIAEQIAGHPEVTFKG 320
Cdd:PRK13512 240 HPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 321 YVGANIVKFFDYTLASTGISPQELKNFDYQMVEVNLYTHAGYYPGNSKVHLRAYFDKETRRILRAAAVGQKDVDKRIDVL 400
Cdd:PRK13512 320 FLGNNIVKFFDYTFASVGVKPNELKQFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRKILRAAAVGKEGADKRIDVL 399
|
410 420 430
....*....|....*....|....*....|....*....
gi 504427289 401 TMALMHQATIDELTEFEVAYAPPFAHPKDLINMLGYKAR 439
Cdd:PRK13512 400 SMAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK 438
|
|
| CoA_CoA_reduc |
TIGR03385 |
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1. ... |
16-435 |
0e+00 |
|
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1.14), as characterized in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi, and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol. [Cellular processes, Detoxification]
Pssm-ID: 163244 [Multi-domain] Cd Length: 427 Bit Score: 558.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 16 TSASQIRRLDKDSRITVYEKDSFMSFANCGLPYYLGNVIEERDDILSTNPEKFKAYKDIDVKVKHEVLKIDDKKQTVTVK 95
Cdd:TIGR03385 1 SAASRVRRLDKESDIIVFEKTEDVSFANCGLPYVIGGVIDDRNKLLAYTPEVFIKKRGIDVKTNHEVIEVNDERQTVVVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 96 NHFTGETFEDAYDALVLSPGARASQLNF---DVPHLFTLRNMDDTDQIDTYIRQYNVKTVLIVGAGYVSLEMVENMHHRG 172
Cdd:TIGR03385 81 NNKTNETYEESYDYLILSPGASPIVPNIegiNLDIVFTLRNLEDTDAIKQYIDKNKVENVVIIGGGYIGIEMAEALRERG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 173 LHPTLIHRSEAV-NKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGH--TVTFTSGAVEDYDLIIAGVGVRPNSEFIQN 249
Cdd:TIGR03385 161 KNVTLIHRSERIlNKLFDEEMNQIVEEELKKHEINLRLNEEVDSIEGEerVKVFTSGGVYQADMVILATGIKPNSELAKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 250 SGIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSFYRHVDLPAHVPLAWGAHRGASIIAEQIAGHpEVTFKGYVGANIVKF 329
Cdd:TIGR03385 241 SGLKLGETGAIWVNEKFQTSVPNIYAAGDVAESHNIITKKPAWVPLAWGANKMGRIAGENIAGN-DIEFKGVLGTNITKF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 330 FDYTLASTGISPQELK--NFDYQMVEVNLYTHAGYYPGNSKVHLRAYFDKETRRILRAAAVGQKDVDKRIDVLTMALMHQ 407
Cdd:TIGR03385 320 FDLTIASTGVTENEAKklNIDYKTVFVKAKTHANYYPGNSPLHLKLIYEKDTRRILGAQAVGKEGADKRIDVLAAAIMAG 399
|
410 420
....*....|....*....|....*...
gi 504427289 408 ATIDELTEFEVAYAPPFAHPKDLINMLG 435
Cdd:TIGR03385 400 LTVKDLFFFELAYAPPYSRVWDPLNMAG 427
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
3-439 |
2.56e-113 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 340.09 E-value: 2.56e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 3 KHIIVVGAVAGGATSASQIRRLDKDSRITVYEKDSFMSFANCGLPYYLGNVIEERDDILSTNPEKFKAyKDIDVKVKHEV 82
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIK-SGIDVKTEHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 83 LKIDDKKQTVTVKNHFTGETFEDAYDALVLSPGARA---SQLNFDVPHLFTLRNMDDTDQIDTYIRQYNVKTVLIVGAGY 159
Cdd:PRK09564 80 VKVDAKNKTITVKNLKTGSIFNDTYDKLMIATGARPiipPIKNINLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 160 VSLEMVENMHHRGLHPTLIHRSEAV-NKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGH---TVTFTSGAVEDYDLII 235
Cdd:PRK09564 160 IGLEAVEAAKHLGKNVRIIQLEDRIlPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEdkvEGVVTDKGEYEADVVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 236 AGVGVRPNSEFIQNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSFYRHVDLPAHVPLAWGAHRGASIIAEQIAGHpE 315
Cdd:PRK09564 240 VATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGR-H 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 316 VTFKGYVGANIVKFFDYTLASTGISPQELK--NFDYQMVEVNLYTHAGYYPGNSKVHLRAYFDKETRRILRAAAVGQKDV 393
Cdd:PRK09564 319 VSFKGTLGSACIKVLDLEAARTGLTEEEAKklGIDYKTVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKKGA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 504427289 394 DKRIDVLTMALMHQATIDELTEFEVAYAPPFAHPKDLINMLGYKAR 439
Cdd:PRK09564 399 VLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVAGNVAK 444
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
23-338 |
3.06e-107 |
|
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: 319.83 E-value: 3.06e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 23 RLDKDSRITVYEKDSFMSFANCGLPYYLGNVIEERDDILSTNPEKFKAYkDIDVKVKHEVLKIDDKKQTVTVKnhfTGET 102
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERK-GIDVRTGTEVTAIDPEAKTVTLR---DGET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 103 FedAYDALVLSPGARASQLNF---DVPHLFTLRNMDDTDQIDTYIRQYNVKTVLIVGAGYVSLEMVENMHHRGLHPTLIH 179
Cdd:COG0446 77 L--SYDKLVLATGARPRPPPIpglDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 180 RSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGH---TVTFTSGAVEDYDLIIAGVGVRPNSEFIQNSGIQLDA 256
Cdd:COG0446 155 RAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDdkvAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 257 KGYIPVNDKFETNIPNIYAVGDIVTSFYRHVDLPAHVPLAWGAHRGASIIAEQIAGHPEvTFKGyVGANIVKFFDYTLAS 336
Cdd:COG0446 235 RGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPA-PFPG-LGTFISKVFDLCIAS 312
|
..
gi 504427289 337 TG 338
Cdd:COG0446 313 TG 314
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
2-339 |
5.70e-63 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 208.46 E-value: 5.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 2 KKHIIVVGAVAGGATSASQIRRLDKDSRITVYEKDSFMSFANCGLPYYLGNVIEERDdiLSTNPEKFKAYKDIDVKVKHE 81
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEED--LLLRPADFYEENGIDLRLGTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 82 VLKIDDKKQTVTVKNhftGETFedAYDALVLSPGARASQLNF---DVPHLFTLRNMDDTDQIDTYIRQynVKTVLIVGAG 158
Cdd:COG1251 79 VTAIDRAARTVTLAD---GETL--PYDKLVLATGSRPRVPPIpgaDLPGVFTLRTLDDADALRAALAP--GKRVVVIGGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 159 YVSLEMVENMHHRGLHPTLIHRSEAV-NKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDG----HTVTFTSGAVEDYDL 233
Cdd:COG1251 152 LIGLEAAAALRKRGLEVTVVERAPRLlPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGddrvTGVRLADGEELPADL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 234 IIAGVGVRPNSEFIQNSGIQLDaKGyIPVNDKFETNIPNIYAVGDIVTSFYRHVDLP--AHVPLAWgahRGASIIAEQIA 311
Cdd:COG1251 232 VVVAIGVRPNTELARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRvlELVAPAY---EQARVAAANLA 306
|
330 340
....*....|....*....|....*...
gi 504427289 312 GHPEvTFKGYVGANIVKFFDYTLASTGI 339
Cdd:COG1251 307 GGPA-AYEGSVPSTKLKVFGVDVASAGD 333
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
3-298 |
4.39e-48 |
|
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: 166.72 E-value: 4.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 3 KHIIVVGAVAGGATSASQIRRLDKdsRITVYEKDSFMSFANCGLPYYLGNVIEERDDILST-------NPEKFKAYKDID 75
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGG--KVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWadlykrkEEVVKKLNNGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 76 VKVKHEVLKIDDKKQTVTVKNHFTGETFEDAYDALVLSPGARASQLN---FDVPHLFTLRNMDDTDqidtYIRQYNV-KT 151
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPipgVELNVGFLVRTLDSAE----ALRLKLLpKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 152 VLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSI----DGHTVTFTSGA 227
Cdd:pfam07992 155 VVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIigdgDGVEVILKDGT 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427289 228 VEDYDLIIAGVGVRPNSEFIQNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIvtsfyrHVDLPAHVPLAWG 298
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC------RVGGPELAQNAVA 299
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
2-338 |
1.48e-39 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 146.05 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 2 KKHIIVVGAVAGGATSASQIRR-LDKDSRITVYEKDSFMSFANcGLPYYLGNVIEERDDILSTNpekfKAYKDIDVKVKH 80
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKkLGGDAEVTLIDPNPYHLFQP-LLPEVAAGTLSPDDIAIPLR----ELLRRAGVRFIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 81 -EVLKIDDKKQTVTVKNhftGETFEdaYDALVLSPGARASqlNFDVP----HLFTLRNMDDT----DQIDTYIRQYNVK- 150
Cdd:COG1252 76 gEVTGIDPEARTVTLAD---GRTLS--YDYLVIATGSVTN--FFGIPglaeHALPLKTLEDAlalrERLLAAFERAERRr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 151 --TVLIVGAGYVSLEMVENMHH--------RGLHP-----TLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKS 215
Cdd:COG1252 149 llTIVVVGGGPTGVELAGELAEllrkllryPGIDPdkvriTLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 216 IDGHTVTFTSGAVEDYDLIIAGVGVRPNsEFIQNSGIQLDAKGYIPVNDKFET-NIPNIYAVGDIVTsfYRHVDLPAHVP 294
Cdd:COG1252 229 VDADGVTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAA--VPDPDGKPVPK 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 504427289 295 LAWGAHRGASIIAEQIA----GHPEVTFkgyvganivKFFDY-TLASTG 338
Cdd:COG1252 306 TAQAAVQQAKVLAKNIAallrGKPLKPF---------RYRDKgCLASLG 345
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
150-427 |
2.11e-33 |
|
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: 130.59 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 150 KTVLIVGAGYVSLEMVeNMHHR-GLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSI----DGHTVTFT 224
Cdd:COG1249 169 KSLVVIGGGYIGLEFA-QIFARlGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVektgDGVTVTLE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 225 SGAVE---DYDLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIVtsfyRHVDLpAHVplawgA 299
Cdd:COG1249 248 DGGGEeavEADKVLVATGRRPNTDGLglEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVT----GGPQL-AHV-----A 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 300 HRGASIIAEQIAGHPEVTFKGYVGANIVkffdYT---LASTGISPQELK--NFDYQMVEVNL----YTHAGyypGNSKVH 370
Cdd:COG1249 318 SAEGRVAAENILGKKPRPVDYRAIPSVV----FTdpeIASVGLTEEEAReaGIDVKVGKFPFaangRALAL---GETEGF 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 504427289 371 LRAYFDKETRRILRAAAVGQkDVDKRIDVLTMALMHQATIDELTEFevayapPFAHP 427
Cdd:COG1249 391 VKLIADAETGRILGAHIVGP-HAGELIHEAALAMEMGLTVEDLADT------IHAHP 440
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
150-427 |
3.44e-27 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 112.96 E-value: 3.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 150 KTVLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYnIPYRLNEEIKSI-----DGHTVTFT 224
Cdd:PRK06292 170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVeksgdEKVEELEK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 225 SGAVED--YDLIIAGVGVRPNSEF--IQNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIVTsfyrhvDLP-AHVplawgA 299
Cdd:PRK06292 249 GGKTETieADYVLVATGRRPNTDGlgLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNG------KPPlLHE-----A 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 300 HRGASIIAEQIAGHPevtfKGYVGANIVKFFDYT---LASTGISPQELK--NFDYQMVEVNlythagyYPGNSKVH---- 370
Cdd:PRK06292 318 ADEGRIAAENAAGDV----AGGVRYHPIPSVVFTdpqIASVGLTEEELKaaGIDYVVGEVP-------FEAQGRARvmgk 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427289 371 ----LRAYFDKETRRILRAAAVGqKDVDKRIDVLTMALMHQATIDELTEFevayapPFAHP 427
Cdd:PRK06292 387 ndgfVKVYADKKTGRLLGAHIIG-PDAEHLIHLLAWAMQQGLTVEDLLRM------PFYHP 440
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
1-278 |
7.34e-25 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 105.38 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 1 MKKHIIVVGAvaGGAtsASQ----IRRLDKDSRITVYEKDSfmsfancGLPYY---LGNVIEER---DDILSTNPEKFKA 70
Cdd:PRK04965 1 MSNGIVIIGS--GFA--ARQlvknIRKQDAHIPITLITADS-------GDEYNkpdLSHVFSQGqraDDLTRQSAGEFAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 71 YKDIDVKVKHEVLKIDDKKQTVTVKnhftGETFedAYDALVLSPGARAsqlnFdVP------HLFTLRNMDDTDQIDTYI 144
Cdd:PRK04965 70 QFNLRLFPHTWVTDIDAEAQVVKSQ----GNQW--QYDKLVLATGASA----F-VPpipgreLMLTLNSQQEYRAAETQL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 145 RQynVKTVLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAV-NKLMDQDMNSVIFDALNQYNIPYRLNEEIKSI----DGH 219
Cdd:PRK04965 139 RD--AQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLlASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLektdSGI 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 504427289 220 TVTFTSGAVEDYDLIIAGVGVRPNSEFIQNSGIQLdAKGyIPVNDKFETNIPNIYAVGD 278
Cdd:PRK04965 217 RATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAV-NRG-IVVDSYLQTSAPDIYALGD 273
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
81-303 |
2.77e-23 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 99.42 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 81 EVLKIDDKKQTVTVKNHfTGETFEdAyDALVLSPGARASQLNFDVPHLFTLRN------MDdtdqidtyIRQYNVKTVLI 154
Cdd:COG0492 78 EVTSVDKDDGPFRVTTD-DGTEYE-A-KAVIIATGAGPRKLGLPGEEEFEGRGvsycatCD--------GFFFRGKDVVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 155 VGAGYVSLEMVENMHHRGLHPTLIHRSE---AVNKLMDQdmnsvifdALNQYNIPYRLNEEIKSIDG----HTVTFT--- 224
Cdd:COG0492 147 VGGGDSALEEALYLTKFASKVTLIHRRDelrASKILVER--------LRANPKIEVLWNTEVTEIEGdgrvEGVTLKnvk 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 225 SGAVEDYD---LIIAgVGVRPNSEFIQNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSFYRHVdlpahvplAWGAHR 301
Cdd:COG0492 219 TGEEKELEvdgVFVA-IGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQA--------ATAAGE 289
|
..
gi 504427289 302 GA 303
Cdd:COG0492 290 GA 291
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
89-389 |
8.99e-22 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 97.14 E-value: 8.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 89 KQTVTVKNHFTGETFEdaYDALVLSPGARAsqlnfdvphlFTLRNMD-DTDQIDTYIRQYNVKTV----LIVGAGYVSLE 163
Cdd:PRK06416 119 PNTVRVMTEDGEQTYT--AKNIILATGSRP----------RELPGIEiDGRVIWTSDEALNLDEVpkslVVIGGGYIGVE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 164 MVENMHHRGLHPTLIhrsEAVNKLM---DQDMNSVIFDALNQYNIPYRLNEEIKSI----DGHTVTFTSGAVEDY---DL 233
Cdd:PRK06416 187 FASAYASLGAEVTIV---EALPRILpgeDKEISKLAERALKKRGIKIKTGAKAKKVeqtdDGVTVTLEDGGKEETleaDY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 234 IIAGVGVRPNSEFI--QNSGIQLDaKGYIPVNDKFETNIPNIYAVGDIvtsfyrhvdlpahVPLAWGAHRG---ASIIAE 308
Cdd:PRK06416 264 VLVAVGRRPNTENLglEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI-------------VGGPMLAHKAsaeGIIAAE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 309 QIAGHP-EVTfkgYVGANIVKFFDYTLASTGISPQELKNFDYQmVEVNLYthagYYPGNSKV--------HLRAYFDKET 379
Cdd:PRK06416 330 AIAGNPhPID---YRGIPAVTYTHPEVASVGLTEAKAKEEGFD-VKVVKF----PFAGNGKAlalgetdgFVKLIFDKKD 401
|
330
....*....|
gi 504427289 380 RRILRAAAVG 389
Cdd:PRK06416 402 GEVLGAHMVG 411
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
5-338 |
1.54e-21 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 97.59 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 5 IIVVGAVAGGATSASQIRRLDKDS-RITVYEKDSFMSFANCGLPYYLGNviEERDDILSTNPEKFKAYKDIDVKVKHEVL 83
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSVLQG--EADLDDITLNSKDWYEKHGITLYTGETVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 84 KID-DKKQTVTVKnhftGETFedAYDALVLSPGARASQLNF---DVPHLFTLRNMDDTDQIDTYIRQYnvKTVLIVGAGY 159
Cdd:TIGR02374 79 QIDtDQKQVITDA----GRTL--SYDKLILATGSYPFILPIpgaDKKGVYVFRTIEDLDAIMAMAQRF--KKAAVIGGGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 160 VSLEMVENMHHRGLHPTLIHRSEAV-NKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGHT----VTFTSGAVEDYDLI 234
Cdd:TIGR02374 151 LGLEAAVGLQNLGMDVSVIHHAPGLmAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATkadrIRFKDGSSLEADLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 235 IAGVGVRPNSEFIQNSGIqlDAKGYIPVNDKFETNIPNIYAVGDIVTSFYRHVDLPAhvPLawgaHRGASIIAEQIAGHP 314
Cdd:TIGR02374 231 VMAAGIRPNDELAVSAGI--KVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVA--PL----YEQAKVLADHICGVE 302
|
330 340
....*....|....*....|....
gi 504427289 315 EVTFKGYVGANIVKFFDYTLASTG 338
Cdd:TIGR02374 303 CEEYEGSDLSAKLKLLGVDVWSAG 326
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
150-279 |
7.70e-21 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 94.45 E-value: 7.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 150 KTVLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSI----DGH-TVTFT 224
Cdd:PRK06116 168 KRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVeknaDGSlTLTLE 247
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504427289 225 SGAVEDYDLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVNDKFETNIPNIYAVGDI 279
Cdd:PRK06116 248 DGETLTVDCLIWAIGREPNTDGLglENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
154-346 |
2.94e-19 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 89.60 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 154 IVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSI----DGHTVTFTSGA-- 227
Cdd:PRK06327 188 VIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIktggKGVSVAYTDADge 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 228 --VEDYDLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSFyrhvdLPAHVplawGAHRGA 303
Cdd:PRK06327 268 aqTLEVDKLIVSIGRVPNTDGLglEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGP-----MLAHK----AEEEGV 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504427289 304 sIIAEQIAGHpevtfKGYVGANIVKFFDYT---LASTGISPQELKN 346
Cdd:PRK06327 339 -AVAERIAGQ-----KGHIDYNTIPWVIYTspeIAWVGKTEQQLKA 378
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
153-427 |
3.83e-19 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 89.49 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 153 LIVGAGYVSLEMVEnMHHR-GLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSI----DGHTVTFTSGA 227
Cdd:PRK06370 175 VIIGGGYIGLEFAQ-MFRRfGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVerdgDGIAVGLDCNG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 228 VEDY---DLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSF-YRHVdlpahvplawgAHR 301
Cdd:PRK06370 254 GAPEitgSHILVAVGRVPNTDDLglEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGaFTHT-----------AYN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 302 GASIIAEQIAGHPEVTfkgyVGANIVKFFDYT---LASTGISPQELKN-------FDYQMVEVNLYTHAGYYPGNSKVHL 371
Cdd:PRK06370 323 DARIVAANLLDGGRRK----VSDRIVPYATYTdppLARVGMTEAEARKsgrrvlvGTRPMTRVGRAVEKGETQGFMKVVV 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 504427289 372 rayfDKETRRILRAAAVGqKDVDKRIDVLTMALMHQATIDELTEfevayaPPFAHP 427
Cdd:PRK06370 399 ----DADTDRILGATILG-VHGDEMIHEILDAMYAGAPYTTLSR------AIHIHP 443
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
3-314 |
5.37e-17 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 82.28 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 3 KHIIVVGAVAGGATSASQIRRLDKDSRITVYEKDSFMSFANCGLPY-YLgnvIEERDDILSTNPEKFKAYKDIDVKVKHE 81
Cdd:PRK09754 4 KTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKsML---LEDSPQLQQVLPANWWQENNVHLHSGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 82 VLKIDDKKQTVTVKNhftGETFEdaYDALVLSPGARASQLnfdvPHL-------FTLRNMDDTDQIDTYIRQYnvKTVLI 154
Cdd:PRK09754 81 IKTLGRDTRELVLTN---GESWH--WDQLFIATGAAARPL----PLLdalgercFTLRHAGDAARLREVLQPE--RSVVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 155 VGAGYVSLEMVENMHHRGLHPTLIhrsEAVNKLMDQDMNSVIFDAL----NQYNIPYRLNEEIKSI-DGHTV--TFTSGA 227
Cdd:PRK09754 150 VGAGTIGLELAASATQRRCKVTVI---ELAATVMGRNAPPPVQRYLlqrhQQAGVRILLNNAIEHVvDGEKVelTLQSGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 228 VEDYDLIIAGVGVRPNSEFIQNSGiqLDAKGYIPVNDKFETNIPNIYAVGDIVTSFYRHVDLpaHVPLAW-GAHRGASII 306
Cdd:PRK09754 227 TLQADVVIYGIGISANDQLAREAN--LDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGAL--HRCESWeNANNQAQIA 302
|
....*...
gi 504427289 307 AEQIAGHP 314
Cdd:PRK09754 303 AAAMLGLP 310
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
150-279 |
4.52e-15 |
|
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: 76.94 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 150 KTVLIVGAGYVSLEM--VENMHH-RGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGHT-----V 221
Cdd:TIGR01423 188 RRVLTVGGGFISVEFagIFNAYKpRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNAdgskhV 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 222 TFTSGAVEDYDLIIAGVGVRPNSEFIQ--NSGIQLDAKGYIPVNDKFETNIPNIYAVGDI 279
Cdd:TIGR01423 268 TFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGDV 327
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
152-226 |
4.56e-14 |
|
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: 67.23 E-value: 4.56e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427289 152 VLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGH----TVTFTSG 226
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNgdgvVVVLTDG 80
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
81-280 |
1.01e-13 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 72.88 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 81 EVLKIDDKKQTVTVKNhftgetfedaydaLVLSPG---ARASQLNFDVPHLFtlrnmdDTDQIDTYirQYNVKTVLIVGA 157
Cdd:PRK05249 125 EVECPDGEVETLTADK-------------IVIATGsrpYRPPDVDFDHPRIY------DSDSILSL--DHLPRSLIIYGA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 158 GYVSLE---MVENMhhrGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGH----TVTFTSGAVED 230
Cdd:PRK05249 184 GVIGCEyasIFAAL---GVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGddgvIVHLKSGKKIK 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504427289 231 YDLIIAGVGVRPNSEF--IQNSGIQLDAKGYIPVNDKFETNIPNIYAVGDIV 280
Cdd:PRK05249 261 ADCLLYANGRTGNTDGlnLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVI 312
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
150-301 |
2.78e-12 |
|
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: 68.34 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 150 KTvLIVGAGYVSLEMVENMHHRGLHPTLIHRSeAVNKLMDQDMNSVIFDALNQYNIPYR---LNEEIKSIDGHT-VTFT- 224
Cdd:TIGR01438 182 KT-LVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDCANKVGEHMEEHGVKFKrqfVPIKVEQIEAKVlVEFTd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 225 --SGAVEDYDLIIAGVGVRPNSEFI--QNSGIQLDAK-GYIPVNDKFETNIPNIYAVGDIVTsfyrhvDLPAHVPLAWGA 299
Cdd:TIGR01438 260 stNGIEEEYDTVLLAIGRDACTRKLnlENVGVKINKKtGKIPADEEEQTNVPYIYAVGDILE------DKPELTPVAIQA 333
|
..
gi 504427289 300 HR 301
Cdd:TIGR01438 334 GR 335
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
141-280 |
7.82e-11 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 63.87 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 141 DTYIRQYNVKTVLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNI-------PYRLnEEI 213
Cdd:PTZ00058 229 DDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELENDMKKNNIniithanVEEI-EKV 307
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427289 214 KSIDGHTVTFTSGAVEDYDLIIAGVGVRPNSEFIQNSGIQ-LDAKGYIPVNDKFETNIPNIYAVGDIV 280
Cdd:PTZ00058 308 KEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNiKTPKGYIKVDDNQRTSVKHIYAVGDCC 375
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
152-287 |
3.49e-10 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 61.51 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 152 VLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFD-ALNQYNIpyRLNEEIKSI----DGHTVTFTSG 226
Cdd:PRK07846 169 LVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTElASKRWDV--RLGRNVVGVsqdgSGVTLRLDDG 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427289 227 AVEDYDLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVnDKFE-TNIPNIYAVGDiVTSFY--RHV 287
Cdd:PRK07846 247 STVEADVLLVATGRVPNGDLLdaAAAGVDVDEDGRVVV-DEYQrTSAEGVFALGD-VSSPYqlKHV 310
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
150-279 |
4.77e-10 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 61.37 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 150 KTVLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYR----LNEEIKSIDGHTVTFTS 225
Cdd:PLN02507 204 KRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHprtnLTQLTKTEGGIKVITDH 283
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504427289 226 GAVEDYDLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVNDKFETNIPNIYAVGDI 279
Cdd:PLN02507 284 GEEFVADVVLFATGRAPNTKRLnlEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
1-407 |
4.87e-10 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 61.30 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 1 MKKH-IIVVGAVAGGATSASQIRRLDKdsRITVYEKDSFMSFANC-----------------GLPYylGNVIEERDDILS 62
Cdd:PRK07251 1 MLTYdLIVIGFGKAGKTLAAKLASAGK--KVALVEESKAMYGGTCinigciptktllvaaekNLSF--EQVMATKNTVTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 63 T-NPEKFKAYKDIDVK--------VKHEVLKI---DDKKQtvtvknhFTGETfedaydaLVLSPGARASQLNfdVPHLFT 130
Cdd:PRK07251 77 RlRGKNYAMLAGSGVDlydaeahfVSNKVIEVqagDEKIE-------LTAET-------IVINTGAVSNVLP--IPGLAD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 131 LRNMDDTDQIDTYIRQynVKTVLIVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLN 210
Cdd:PRK07251 141 SKHVYDSTGIQSLETL--PERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 211 ---EEIKSIDGHTVTFTSGAVEDYDLIIAGVGVRPNSEFIQ--NSGIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSfyr 285
Cdd:PRK07251 219 ahtTEVKNDGDQVLVVTEDETYRFDALLYATGRKPNTEPLGleNTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGG--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 286 hvdlPAHVPLAWGAHRgasIIAEQIAGHPEVTFKGYVGANIVKFFDYTLASTGISPQELKNFDYQmVEVNLYTHAGYYPG 365
Cdd:PRK07251 296 ----PQFTYISLDDFR---IVFGYLTGDGSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLP-YAVKELLVAAMPRA 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 504427289 366 NSKVHLRAYF----DKETRRILRAAAVGQkDVDKRIDVLTMALMHQ 407
Cdd:PRK07251 368 HVNNDLRGAFkvvvNTETKEILGATLFGE-GSQEIINLITMAMDNK 412
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
150-362 |
1.15e-08 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 57.14 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 150 KTvLIVGAGYVSLEMVENMHHRGLHPTLIHRSeAVNKLMDQDMNSVIFDALNQYNIPY----------RLNEEIKsidgh 219
Cdd:PTZ00052 184 KT-LIVGASYIGLETAGFLNELGFDVTVAVRS-IPLRGFDRQCSEKVVEYMKEQGTLFlegvvpinieKMDDKIK----- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 220 tVTFTSGAVEDYDLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVNDKfETNIPNIYAVGDIVtsfyrhVDLPAHVPLAW 297
Cdd:PTZ00052 257 -VLFSDGTTELFDTVLYATGRKPDIKGLnlNAIGVHVNKSNKIIAPND-CTNIPNIFAVGDVV------EGRPELTPVAI 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427289 298 GAhrgASIIAEQIAGHPEvtfkgyvganivKFFDYTLASTGIspqelknfdYQMVEvnlYTHAGY 362
Cdd:PTZ00052 329 KA---GILLARRLFKQSN------------EFIDYTFIPTTI---------FTPIE---YGACGY 366
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
216-310 |
2.15e-08 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 56.29 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 216 IDGHTVTFtsgaveDYDLIIAGVGVRPNSeFIQNS--GIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSfyrhvdlPAHV 293
Cdd:PRK12778 666 IPGSTFTV------DVDLVIVSVGVSPNP-LVPSSipGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRG-------GATV 731
|
90
....*....|....*...
gi 504427289 294 PLAWGA-HRGASIIAEQI 310
Cdd:PRK12778 732 ILAMGDgKRAAAAIDEYL 749
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
327-425 |
4.06e-08 |
|
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: 51.02 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 327 VKFFDYTLASTGISPQELKNFDYQMVEVNLY----THAGYYPGNsKVHLRAYFDKETRRILRAAAVGqKDVDKRIDVLTM 402
Cdd:pfam02852 4 VVFTDPEIASVGLTEEEAKEKGGEVKVGKFPfaanGRALAYGDT-DGFVKLVADRETGKILGAHIVG-PNAGELIQEAAL 81
|
90 100
....*....|....*....|...
gi 504427289 403 ALMHQATIDELTEfEVAYAPPFA 425
Cdd:pfam02852 82 AIKMGATVEDLAN-TIHIHPTLS 103
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
70-277 |
5.40e-08 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 54.15 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 70 AYKDIDVKVKHEVLKIddKKQtvtvKNHFTGETFEDAYDA--LVLSPGarasqlNFDVPHLftlrnMDDTDQIDTY---- 143
Cdd:pfam13738 86 DHFELPINLFEEVTSV--KKE----DDGFVVTTSKGTYQAryVIIATG------EFDFPNK-----LGVPELPKHYsyvk 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 144 -IRQYNVKTVLIVGaGYVS-----LEMVEnmhhRGLHPTLIHRSEAVNKLMDQDMNSV-------IFDALNQYNIPYRLN 210
Cdd:pfam13738 149 dFHPYAGQKVVVIG-GYNSavdaaLELVR----KGARVTVLYRGSEWEDRDSDPSYSLspdtlnrLEELVKNGKIKAHFN 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427289 211 EEIKSID----GHTVTFTSG-AVEDYDLIIAGVGVRPNSEFIQNSGIQLDAKGYIPVNDK-FETNIPNIYAVG 277
Cdd:pfam13738 224 AEVKEITevdvSYKVHTEDGrKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
53-312 |
5.94e-08 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 54.77 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 53 VIEERDDILSTNPEKF---KAYkDIDVKVKHEVLKIDDKKQTVTVKnhftgeTFEDAYDALVLSPGARASqlNFDVP--- 126
Cdd:PTZ00318 64 ICEPVRPALAKLPNRYlraVVY-DVDFEEKRVKCGVVSKSNNANVN------TFSVPYDKLVVAHGARPN--TFNIPgve 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 127 -HLFTLRNMDDTDQIDTYIRQ---------------YNVKTVLIVGAGYVSLEMVENMHH------RGLHP--------T 176
Cdd:PTZ00318 135 eRAFFLKEVNHARGIRKRIVQcieraslpttsveerKRLLHFVVVGGGPTGVEFAAELADffrddvRNLNPelveeckvT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 177 LIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEEIKSIDGHTVTFTSGAVEDYDLIIAGVGVRPNSeFIQNSGIQLDA 256
Cdd:PTZ00318 215 VLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVWSTGVGPGP-LTKQLKVDKTS 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 504427289 257 KGYIPVNDKFET-NIPNIYAVGDIVTSfyRHVDLPahvPLAWGAHRGASIIAEQIAG 312
Cdd:PTZ00318 294 RGRISVDDHLRVkPIPNVFALGDCAAN--EERPLP---TLAQVASQQGVYLAKEFNN 345
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
150-279 |
1.59e-07 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 53.34 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 150 KTVLIVGAGYVSLEMVENMHhrGLHpTLIH---RSEAVNKLMDQDMNSVIFDALNQYNIPYRLNEE----IKSIDGHTVT 222
Cdd:PLN02546 253 EKIAIVGGGYIALEFAGIFN--GLK-SDVHvfiRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESpqaiIKSADGSLSL 329
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 223 FTS-GAVEDYDLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVNDKFETNIPNIYAVGDI 279
Cdd:PLN02546 330 KTNkGTVEGFSHVMFATGRKPNTKNLglEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDV 389
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
232-281 |
4.88e-07 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 51.67 E-value: 4.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 504427289 232 DLIIAGVGVRPNSEFIQNS-GIQLDAKGYIPVNDK-FETNIPNIYAVGDIVT 281
Cdd:COG0493 361 DLVILAIGQTPDPSGLEEElGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVR 412
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
232-281 |
3.60e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 49.02 E-value: 3.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 504427289 232 DLIIAGVGVRPNSEFIQNS-GIQLDAKGYIPVNDK-FETNIPNIYAVGDIVT 281
Cdd:PRK11749 377 DLVIKAIGQTPNPLILSTTpGLELNRWGTIIADDEtGRTSLPGVFAGGDIVT 428
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
79-286 |
1.07e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 47.36 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 79 KHEVLKIDDKKQTVTVKNH---FTGETFEDAYDALVLSPGARASQLNFDVPHLFTLRNMDDTDQIDTYIrqYNVKTVLIV 155
Cdd:PRK10262 75 KFETEIIFDHINKVDLQNRpfrLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFF--YRNQKVAVI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 156 GAGYVSLEMVENMHHRGLHPTLIHRSEAVNKlmDQDMNSVIFDALNQYNIPYRLNEEIKSIDGHTVTFTSGAVEDYD--- 232
Cdd:PRK10262 153 GGGNTAVEEALYLSNIASEVHLIHRRDGFRA--EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQnsd 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427289 233 ----LIIAG----VGVRPNSEFIQNSgIQLDaKGYIPVN-----DKFETNIPNIYAVGDIVTSFYRH 286
Cdd:PRK10262 231 niesLDVAGlfvaIGHSPNTAIFEGQ-LELE-NGYIKVQsgihgNATQTSIPGVFAAGDVMDHIYRQ 295
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
154-279 |
1.75e-05 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 46.93 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 154 IVGAGYVSLEMVENMHHRGLHPTLIHRSEAVNKLMDQDMNSVIFDALNQYNIPYRLN---EEIKSIDGHTVTFTSGAVED 230
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNahvERISHHENQVQVHSEHAQLA 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504427289 231 YDLIIAGVGVRPNSEFI--QNSGIQLDAKGYIPVNDKFETNIPNIYAVGDI 279
Cdd:PRK08010 243 VDALLIASGRQPATASLhpENAGIAVNERGAIVVDKYLHTTADNIWAMGDV 293
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
61-278 |
5.62e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 45.49 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 61 LSTNPEKFKAYKDIDVKVKHEVLKIDDKKQTVTVKnhfTGETFEdaYDALVLSPGA-------RASqlnfDVPHLFTLRN 133
Cdd:PRK14989 61 LSLVREGFYEKHGIKVLVGERAITINRQEKVIHSS---AGRTVF--YDKLIMATGSypwippiKGS----ETQDCFVYRT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 134 MDDTDQIDTYIRQynVKTVLIVGAGYVSLEMVENMHHRGLHptlIHRSEAVNKLMDQDMNSVIFDALNQ----YNIPYRL 209
Cdd:PRK14989 132 IEDLNAIEACARR--SKRGAVVGGGLLGLEAAGALKNLGVE---THVIEFAPMLMAEQLDQMGGEQLRRkiesMGVRVHT 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427289 210 NEEIKSI------DGHTVTFTSGAVEDYDLIIAGVGVRPNSEFIQNSGIQLDAKGYIPVNDKFETNIPNIYAVGD 278
Cdd:PRK14989 207 SKNTLEIvqegveARKTMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
224-284 |
2.47e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 43.22 E-value: 2.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427289 224 TSGAVEDYDLiiAGV----GVRPNSEFIQNSgIQLDAKGYIPVNDKFETNIPNIYAVGDIVTSFY 284
Cdd:PRK15317 429 TTGEEHHLEL--EGVfvqiGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVPY 490
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
217-278 |
2.88e-04 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 42.92 E-value: 2.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427289 217 DGHTVTFTSG-AVEDYDLIIAgVGVRPNSEFI--QNSGIQLDAKGYIPVNDKFETNIPNIYAVGD 278
Cdd:PRK07845 249 DGVVVTLTDGrTVEGSHALMA-VGSVPNTAGLglEEAGVELTPSGHITVDRVSRTSVPGIYAAGD 312
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
230-303 |
4.47e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 42.31 E-value: 4.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427289 230 DYDLIIAGVGVRPNSEFIQNS-GIQLDAKGYIPVN-DKFETNIPNIYAVGDIVTSfyrhvdlPAHVPLAWGAHRGA 303
Cdd:PRK12831 384 EVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADeETGLTSKEGVFAGGDAVTG-------AATVILAMGAGKKA 452
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
233-278 |
7.57e-04 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 41.68 E-value: 7.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 504427289 233 LIIAgVGVRPN--SEFIQNSGIQLDAKGYIPVNDKFETNIPNIYAVGD 278
Cdd:PRK13748 357 LLVA-TGRAPNtrSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGD 403
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
196-311 |
9.86e-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: 41.39 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427289 196 IFDALNQYNIPyRLNEEIKSIDGHTVTFTSGAVEDYDLIIAGVGVRPNSEFIQNSGIqLDAKGYipvnDKFET------- 268
Cdd:COG2072 274 YYEALRRGNVE-LVTGGIERITEDGVVFADGTEHEVDVIVWATGFRADLPWLAPLDV-RGRDGR----SGPRAylgvvvp 347
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 504427289 269 NIPNIYAVGdivtsFYRhvdLPAHVPLAWGAHRGASIIAEQIA 311
Cdd:COG2072 348 GFPNLFFLG-----PNS---PSGHSSLTLGAERQARYIARLIA 382
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
191-236 |
8.80e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 38.00 E-value: 8.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 504427289 191 DMNSVIFDALNQYNIPYRLNEEIKSI----DGHTVTFTSGAVEDYDLIIA 236
Cdd:COG0654 105 DLERALLEAARALGVELRFGTEVTGLeqdaDGVTVTLADGRTLRADLVVG 154
|
|
| |
