|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
142-505 |
5.99e-132 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 388.35 E-value: 5.99e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 142 EMLRREQFAGEIVMLSSEAEAPVDRPNLSKdYLAGSAQADWIPLRSGDFYRDLKIDLRLGVEADSIDVAGQAVVLKDGAR 221
Cdd:COG1251 18 EELRKLDPDGEITVIGAEPHPPYNRPPLSK-VLAGETDEEDLLLRPADFYEENGIDLRLGTRVTAIDRAARTVTLADGET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 222 LAYDRLLLATGAEPNRLPVPGADRPNVHVLRTLADSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVVGPEKI 301
Cdd:COG1251 97 LPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 302 PMERVLGPEMGRCVRALHEEHGVIFHLEEGVSAINE----RGVVLKSGEVIAADLIVSGIGVKPRLTLAEKAGLTIDRGV 377
Cdd:COG1251 177 LLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGddrvTGVRLADGEELPADLVVVAIGVRPNTELARAAGLAVDRGI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 378 VVDRTLQTSAPGIYAAGDIARWPDRHSGENIrVEHWVVAERQGQVVARNMLGAREVF-DAVPFFWSQHYDIPINYVGHAE 456
Cdd:COG1251 257 VVDDYLRTSDPDIYAAGDCAEHPGPVYGRRV-LELVAPAYEQARVAAANLAGGPAAYeGSVPSTKLKVFGVDVASAGDAE 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 881038642 457 KWDEIVVHGEIMAHDCLLEYKLNGKTLAVASIFRDADSLKAAAAMEEGR 505
Cdd:COG1251 336 GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
146-453 |
2.04e-94 |
|
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: 289.40 E-value: 2.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 146 REQFAGEIVMLSSEAEAPVDRPNLSKDYLAGSAQADWIPLRSGDFYRDLKIDLRLGVEADSIDVAGQAVVLKDGARLAYD 225
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 226 RLLLATGAEPNRLPVPGADRPNVHVLRTLADSNAIIA--SAKDARRAVVIGASFIGLEAAASLRARDIEVHVVGPEKIPM 303
Cdd:COG0446 81 KLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREalKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 304 eRVLGPEMGRCVRALHEEHGVIFHLEEGVSAI---NERGVVLKSGEVIAADLIVSGIGVKPRLTLAEKAGLTIDR--GVV 378
Cdd:COG0446 161 -GVLDPEMAALLEEELREHGVELRLGETVVAIdgdDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgWIK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881038642 379 VDRTLQTSAPGIYAAGDIARWPDRHSGENIRVEHWVVAERQGQVVARNMLGAREVFDAVPFFWSQHYDIPINYVG 453
Cdd:COG0446 240 VDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFDLCIASTG 314
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
126-458 |
1.21e-60 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 204.39 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 126 EKIVIVGGGAAGFAAAEMLRREQFAGEIVMLSSEAEAPVDRPNLSKDYLAGSAQADWIpLRSGDFYRDLKIDLRLGVEAD 205
Cdd:PRK09754 4 KTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQ-VLPANWWQENNVHLHSGVTIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 206 SIDVAGQAVVLKDGARLAYDRLLLATGAEPNRLPVPGADRPNVHVLRTLADSNAIIASAKDARRAVVIGASFIGLEAAAS 285
Cdd:PRK09754 83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 286 LRARDIEVHVVGPEKIPMERVLGPEMGRCVRALHEEHGVIFHLEEG-VSAINERGVVLK--SGEVIAADLIVSGIGVKPR 362
Cdd:PRK09754 163 ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAiEHVVDGEKVELTlqSGETLQADVVIYGIGISAN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 363 LTLAEKAGLTIDRGVVVDRTLQTSAPGIYAAGDIA--RWPdrhSGENIRVEHWVVAERQGQVVARNMLGAREVFDAVPFF 440
Cdd:PRK09754 243 DQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAitRLD---NGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWF 319
|
330 340
....*....|....*....|
gi 881038642 441 WSQHYDIPINYVG--HAEKW 458
Cdd:PRK09754 320 WSDQYSDNLQFIGdmRGDDW 339
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
142-429 |
4.85e-58 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 205.83 E-value: 4.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 142 EMLRREQFAGEIVMLSSEAEAPVDRPNLSKdYLAGSAQADWIPLRSGDFYRDLKIDLRLGVEADSIDVAGQAVVLKDGAR 221
Cdd:TIGR02374 16 EVLKLNRHMFEITIFGEEPHPNYNRILLSS-VLQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 222 LAYDRLLLATGAEPNRLPVPGADRPNVHVLRTLADSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVVGPEKI 301
Cdd:TIGR02374 95 LSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 302 PMERVLGPEMGRCVRALHEEHGVIFHLE----EGVSAINERGVVLKSGEVIAADLIVSGIGVKPRLTLAEKAGLTIDRGV 377
Cdd:TIGR02374 175 LMAKQLDQTAGRLLQRELEQKGLTFLLEkdtvEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGI 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 881038642 378 VVDRTLQTSAPGIYAAGDIARWPDRHSGenirvehwVVAE--RQGQVVARNMLG 429
Cdd:TIGR02374 255 IVNDSMQTSDPDIYAVGECAEHNGRVYG--------LVAPlyEQAKVLADHICG 300
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
148-420 |
6.25e-55 |
|
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: 186.37 E-value: 6.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 148 QFAGEIVMLSSEAEAPVDRPNLSKDYLAGSAQADwIPLRSGDFYRDLK---------IDLRLGVEADSIDVAGQAVVLK- 217
Cdd:pfam07992 21 QLGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPE-IASLWADLYKRKEevvkklnngIEVLLGTEVVSIDPGAKKVVLEe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 218 ----DGARLAYDRLLLATGAEPNRLPVPGADRPNVHVLRTLADSNAIIaSAKDARRAVVIGASFIGLEAAASLRARDIEV 293
Cdd:pfam07992 100 lvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALR-LKLLPKRVVVVGGGYIGVELAAALAKLGKEV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 294 HVVGPEKIpMERVLGPEMGRCVRALHEEHGVIFHLEEGVSAINERG----VVLKSGEVIAADLIVSGIGVKPRLTLAEKA 369
Cdd:pfam07992 179 TLIEALDR-LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGdgveVILKDGTEIDADLVVVAIGRRPNTELLEAA 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 881038642 370 GLTIDR--GVVVDRTLQTSAPGIYAAGDIARwpdrhsgenIRVEHWVVAERQG 420
Cdd:pfam07992 258 GLELDErgGIVVDEYLRTSVPGIYAAGDCRV---------GGPELAQNAVAQG 301
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
177-426 |
1.53e-40 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 150.28 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 177 SAQADWIPLRsgDFYRDLKIDLRLGvEADSIDVAGQAVVLKDGARLAYDRLLLATGAEPNRLPVPGAdRPNVHVLRTLAD 256
Cdd:COG1252 54 SPDDIAIPLR--ELLRRAGVRFIQG-EVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGL-AEHALPLKTLED 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 257 SNAI---------IASAKDARRAVVIGASFIGLEAAASL-------------RARDIEVHVVGPEKIPMERvLGPEMGRC 314
Cdd:COG1252 130 ALALrerllaafeRAERRRLLTIVVVGGGPTGVELAGELaellrkllrypgiDPDKVRITLVEAGPRILPG-LGEKLSEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 315 VRALHEEHGVIFHLEEGVSAINERGVVLKSGEVIAADLIVSGIGVKPRlTLAEKAGLTIDRG--VVVDRTLQT-SAPGIY 391
Cdd:COG1252 209 AEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLQVpGHPNVF 287
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 881038642 392 AAGDIARWPDRHsgenirvEHWV-----VAERQGQVVARN 426
Cdd:COG1252 288 AIGDCAAVPDPD-------GKPVpktaqAAVQQAKVLAKN 320
|
|
| Rieske_AIFL_N |
cd03478 |
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ... |
13-106 |
1.69e-39 |
|
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.
Pssm-ID: 239560 [Multi-domain] Cd Length: 95 Bit Score: 138.14 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 13 AGGVELAQFSDGKLLGH-VGDEEVLLVQSGDDIFAVGAHCTHYHGPLADGLVVGNSIRCPWHHACFDLRTGEATRAPAFD 91
Cdd:cd03478 1 AVVCRLSDLGDGEMKEVdVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
|
90
....*....|....*
gi 881038642 92 PIARFKVEQRDGKVF 106
Cdd:cd03478 81 SLPCYEVEVEDGRVY 95
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
196-434 |
3.59e-36 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 139.41 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 196 IDLRLGVEADSIDVAGQAVVLKDGAR-----LAYDRLLLATGAEPNRLPVPGADRPNVHVLRTLADSNAIIASAKDAR-- 268
Cdd:PRK09564 71 IDVKTEHEVVKVDAKNKTITVKNLKTgsifnDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEik 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 269 RAVVIGASFIGLEAAASLRARDIEVHVVGPEKIPMERVLGPEMGRCVRALHEEHGVIFHLEEGVSAI----NERGVVLKS 344
Cdd:PRK09564 151 NIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLigedKVEGVVTDK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 345 GEvIAADLIVSGIGVKPRLTLAEKAGL-TIDRG-VVVDRTLQTSAPGIYAAGDIARWPDRHSGENIRVEHWVVAERQGQV 422
Cdd:PRK09564 231 GE-YEADVVIVATGVKPNTEFLEDTGLkTLKNGaIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRM 309
|
250
....*....|..
gi 881038642 423 VARNMLGAREVF 434
Cdd:PRK09564 310 VGENLAGRHVSF 321
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
166-399 |
6.44e-34 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 131.58 E-value: 6.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 166 RPNLSKDYLAGSAQADWIPLRSGDFYRDLKIDLRLGVEADSIDVAGQaVVLKDGARLAYDRLLLATGAEPNRLPVPGadR 245
Cdd:PRK04965 43 KPDLSHVFSQGQRADDLTRQSAGEFAEQFNLRLFPHTWVTDIDAEAQ-VVKSQGNQWQYDKLVLATGASAFVPPIPG--R 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 246 PNVHVLRTLADSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVVGPEKIPMERVLGPEMG-RCVRALhEEHGV 324
Cdd:PRK04965 120 ELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSsRLQHRL-TEMGV 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881038642 325 IFHLEEGVSAINERG----VVLKSGEVIAADLIVSGIGVKPRLTLAEKAGLTIDRGVVVDRTLQTSAPGIYAAGDIARW 399
Cdd:PRK04965 199 HLLLKSQLQGLEKTDsgirATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEI 277
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
147-434 |
1.16e-31 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 129.47 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 147 EQFagEIVMLSSEAEAPVDRPNLSKdYLAGSAqADWIPLRSGDFYRDLKIDLRLGVEADSIDVAGQAVVLKDGARLAYDR 226
Cdd:PRK14989 29 ANF--DITVFCEEPRIAYDRVHLSS-YFSHHT-AEELSLVREGFYEKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 227 LLLATGAEPNRLPVPGADRPNVHVLRTLADSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVVGPEKIPMERV 306
Cdd:PRK14989 105 LIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 307 LGPEMGRCVRALHEEHGVIFHLEEGVSAINERG------VVLKSGEVIAADLIVSGIGVKPRLTLAEKAGLTIDR--GVV 378
Cdd:PRK14989 185 LDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGvearktMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPrgGIV 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 881038642 379 VDRTLQTSAPGIYAAGDIARWPDRHSGenirvehwVVAE--RQGQVVARNMLGAREVF 434
Cdd:PRK14989 265 INDSCQTSDPDIYAIGECASWNNRVFG--------LVAPgyKMAQVAVDHLLGSENAF 314
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
214-438 |
1.19e-30 |
|
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: 124.04 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 214 VVLKDGARLAYDRLLLATGAEPNRLPVPGADRPNVHvlrtlaDSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEV 293
Cdd:COG1249 121 VEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVL------TSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 294 HVVGPekipMERVLG---PEMGRCVRALHEEHGVIFHLEEGVSAINERG----VVLKSG---EVIAADLIVSGIGVKPRL 363
Cdd:COG1249 195 TLVER----GDRLLPgedPEISEALEKALEKEGIDILTGAKVTSVEKTGdgvtVTLEDGggeEAVEADKVLVATGRRPNT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 364 TL--AEKAGLTIDR--GVVVDRTLQTSAPGIYAAGDIA-RWPDRHsgenirvehwvVAERQGQVVARNMLG-AREVFD-- 435
Cdd:COG1249 271 DGlgLEAAGVELDErgGIKVDEYLRTSVPGIYAIGDVTgGPQLAH-----------VASAEGRVAAENILGkKPRPVDyr 339
|
...
gi 881038642 436 AVP 438
Cdd:COG1249 340 AIP 342
|
|
| NirD |
COG2146 |
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ... |
18-109 |
1.51e-27 |
|
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441749 [Multi-domain] Cd Length: 103 Bit Score: 106.08 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 18 LAQFSDGKLLG-HVGDEEVLLVQSGDDIFAVGAHCTHYHGPLADGLVVGNSIRCPWHHACFDLRTGEATRAPAFDPIARF 96
Cdd:COG2146 9 LDDLPEGGGVVvEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLGGPATEPLKTY 88
|
90
....*....|...
gi 881038642 97 KVEQRDGKVFVGD 109
Cdd:COG2146 89 PVRVEDGDVYVDL 101
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
127-433 |
6.22e-26 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 109.87 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 127 KIVIVGGGAAGFAAAEMLRREQFAGEIVMLssEAEAPVDRPNLSKDYLAG---SAQADWIPLRSGDFYRDLKIDLRLGVE 203
Cdd:PRK13512 3 KIIVVGAVAGGATCASQIRRLDKESDIIIF--EKDRDMSFANCALPYYIGevvEDRKYALAYTPEKFYDRKQITVKTYHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 204 ADSIDVAGQAVVLKDGAR-----LAYDRLLLATGAEPNRLPVpgaDRPNVHVLRTLADSNAI--IASAKDARRAVVIGAS 276
Cdd:PRK13512 81 VIAINDERQTVTVLNRKTneqfeESYDKLILSPGASANSLGF---ESDITFTLRNLEDTDAIdqFIKANQVDKALVVGAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 277 FIGLEAAASLRARDIEVHVVG-PEKIpmERVLGPEMGRCVRALHEEHGVIFHLEEGVSAINERGVVLKSGEVIAADLIVS 355
Cdd:PRK13512 158 YISLEVLENLYERGLHPTLIHrSDKI--NKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVEHYDMIIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 356 GIGVKPRLTLAEKAGLTIDRG--VVVDRTLQTSAPGIYAAGDIARWPDRHSGENIRVEHWVVAERQGQVVARNMLGAREV 433
Cdd:PRK13512 236 GVGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTI 315
|
|
| Rieske_RO_ferredoxin |
cd03528 |
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ... |
30-107 |
1.14e-20 |
|
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.
Pssm-ID: 239604 [Multi-domain] Cd Length: 98 Bit Score: 86.77 E-value: 1.14e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881038642 30 VGDEEVLLVQSGDDIFAVGAHCTHYHGPLADGLVVGNSIRCPWHHACFDLRTGEATRAPAFDPIARFKVEQRDGKVFV 107
Cdd:cd03528 20 VGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPATEPLKTYPVKVEDGDVYV 97
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
209-438 |
7.39e-20 |
|
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: 92.10 E-value: 7.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 209 VAGQAVVLKDGARL-AYDRLLLATGAEPNRLPVPGADrpNVHVLrtlaDSNAIIASAKDARRAVVIGASFIGLEAAASLR 287
Cdd:TIGR02053 113 KDPKTVKVDLGREVrGAKRFLIATGARPAIPPIPGLK--EAGYL----TSEEALALDRIPESLAVIGGGAIGVELAQAFA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 288 ARDIEVHVVGPEKIPMERVlGPEMGRCVRALHEEHGVIFHLEEGVSAINERG-------VVLKSGEVIAADLIVSGIGVK 360
Cdd:TIGR02053 187 RLGSEVTILQRSDRLLPRE-EPEISAAVEEALAEEGIEVVTSAQVKAVSVRGggkiitvEKPGGQGEVEADELLVATGRR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 361 P---RLTLaEKAGLTIDR--GVVVDRTLQTSAPGIYAAGDIARWPDRHSgenirvehwvVAERQGQVVARNMLGAREV-- 433
Cdd:TIGR02053 266 PntdGLGL-EKAGVKLDErgGILVDETLRTSNPGIYAAGDVTGGLQLEY----------VAAKEGVVAAENALGGANAkl 334
|
....*.
gi 881038642 434 -FDAVP 438
Cdd:TIGR02053 335 dLLVIP 340
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
203-397 |
1.32e-18 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 86.33 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 203 EADSIDVAGQA--VVLKDGARLAYDRLLLATGAEPNRLPVPGADRPNVHVLRTLADSNAiiASAKDaRRAVVIGASFIGL 280
Cdd:COG0492 78 EVTSVDKDDGPfrVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDG--FFFRG-KDVVVVGGGDSAL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 281 EAAASLRARDIEVHVVgpekipmerVLGPEMgRC----VRALHEEHGVIFHLEEGVSAINE----RGVVLKSG-----EV 347
Cdd:COG0492 155 EEALYLTKFASKVTLI---------HRRDEL-RAskilVERLRANPKIEVLWNTEVTEIEGdgrvEGVTLKNVktgeeKE 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 881038642 348 IAADLIVSGIGVKPRLTLAEKAGLTIDRG--VVVDRTLQTSAPGIYAAGDIA 397
Cdd:COG0492 225 LEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVR 276
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
214-456 |
7.90e-18 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 85.98 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 214 VVLKDGA--RLAYDRLLLATGAEPNRLP-VPgADRPNVHvlrtlaDSNAIIASAKDARRAVVIGASFIGLEAAASLRARD 290
Cdd:PRK05249 126 VECPDGEveTLTADKIVIATGSRPYRPPdVD-FDHPRIY------DSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 291 IEVHVVGPEkipmERVLG---PEMgrcVRAL--H-EEHGVIFHLEEGVSAI--NERGVV--LKSGEVIAAD--LIVSG-I 357
Cdd:PRK05249 199 VKVTLINTR----DRLLSfldDEI---SDALsyHlRDSGVTIRHNEEVEKVegGDDGVIvhLKSGKKIKADclLYANGrT 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 358 GVKPRLTLaEKAGLTID-RG-VVVDRTLQTSAPGIYAAGDIARWPDRHSgenirvehwvVAERQGQVVARNMLGArEVFD 435
Cdd:PRK05249 272 GNTDGLNL-ENAGLEADsRGqLKVNENYQTAVPHIYAVGDVIGFPSLAS----------ASMDQGRIAAQHAVGE-ATAH 339
|
250 260
....*....|....*....|..
gi 881038642 436 AVPFFWSQHYDIP-INYVGHAE 456
Cdd:PRK05249 340 LIEDIPTGIYTIPeISSVGKTE 361
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
218-438 |
3.17e-17 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 84.10 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 218 DGARLAYDRLLLATGAEPNRLPVPGADRPNVHvlrtlaDSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVV- 296
Cdd:PRK06370 128 GGETLRAKRIFINTGARAAIPPIPGLDEVGYL------TNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIe 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 297 -GPEKIPMErvlGPEMGRCVRALHEEHGVIFHLEEGVSAINERG----VVLKSGEV---IAADLIVSGIGVKPR---LTL 365
Cdd:PRK06370 202 rGPRLLPRE---DEDVAAAVREILEREGIDVRLNAECIRVERDGdgiaVGLDCNGGapeITGSHILVAVGRVPNtddLGL 278
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881038642 366 aEKAGLTIDR--GVVVDRTLQTSAPGIYAAGDI-ARWPDRHsgenirvehwvVAERQGQVVARNML--GAREVFDAVP 438
Cdd:PRK06370 279 -EAAGVETDArgYIKVDDQLRTTNPGIYAAGDCnGRGAFTH-----------TAYNDARIVAANLLdgGRRKVSDRIV 344
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
218-439 |
1.08e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 79.45 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 218 DGARLAYDRLLLATGAEpnRLPVPGADRPNVHVLRTladSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVVG 297
Cdd:PRK06292 125 NGERIEAKNIVIATGSR--VPPIPGVWLILGDRLLT---SDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 298 pekipM-ERVLG---PEMGRCVRALHEEHgVIFHLEEGVSAI----NERGVVLKSG---EVIAADLIVSGIGVKPRL-TL 365
Cdd:PRK06292 200 -----RgDRILPledPEVSKQAQKILSKE-FKIKLGAKVTSVeksgDEKVEELEKGgktETIEADYVLVATGRRPNTdGL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 366 A-EKAGLTID-RG-VVVDRTLQTSAPGIYAAGDI-ARWPDRHsgenirvehwvVAERQGQVVARNMLGAREV---FDAVP 438
Cdd:PRK06292 274 GlENTGIELDeRGrPVVDEHTQTSVPGIYAAGDVnGKPPLLH-----------EAADEGRIAAENAAGDVAGgvrYHPIP 342
|
.
gi 881038642 439 F 439
Cdd:PRK06292 343 S 343
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
224-427 |
1.13e-15 |
|
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: 79.02 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 224 YDRLLLATGAE-PNRLPVPGADRPNVH----VLRTLADSNAIIASAKDARRAVVIGASFIGLEAA-ASLRARDIEVHVVg 297
Cdd:COG0493 207 FDAVFLATGAGkPRDLGIPGEDLKGVHsamdFLTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCArTALRLGAESVTIV- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 298 pEKIPMERVlgPEMGRCVRALHEEhGVIFHL----------EEG-VSAIN----ERGVVLKSG-----------EVIAAD 351
Cdd:COG0493 286 -YRRTREEM--PASKEEVEEALEE-GVEFLFlvapveiigdENGrVTGLEcvrmELGEPDESGrrrpvpiegseFTLPAD 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 352 LIVSGIGVKPRLT-LAEKAGLTIDRG--VVVD-RTLQTSAPGIYAAGDIARWPDrhsgeNIrvehwVVAERQGQVVARNM 427
Cdd:COG0493 362 LVILAIGQTPDPSgLEEELGLELDKRgtIVVDeETYQTSLPGVFAGGDAVRGPS-----LV-----VWAIAEGRKAARAI 431
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
218-396 |
1.14e-15 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 79.04 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 218 DGARLAYDRLLLATGAEPNRLPVPGADrpnvHVLrtlaDSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVVG 297
Cdd:PRK06116 126 NGERYTADHILIATGGRPSIPDIPGAE----YGI----TSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 298 PEKIPMeRVLGPEMgrcVRALHEE---HGVIFHLEEGVSAI--NERG---VVLKSGEVIAADLIVSGIGVKPRLT---La 366
Cdd:PRK06116 198 RGDAPL-RGFDPDI---RETLVEEmekKGIRLHTNAVPKAVekNADGsltLTLEDGETLTVDCLIWAIGREPNTDglgL- 272
|
170 180 190
....*....|....*....|....*....|..
gi 881038642 367 EKAGLTID-RG-VVVDRTLQTSAPGIYAAGDI 396
Cdd:PRK06116 273 ENAGVKLNeKGyIIVDEYQNTNVPGIYAVGDV 304
|
|
| Rieske |
cd03467 |
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ... |
23-107 |
1.55e-15 |
|
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.
Pssm-ID: 239550 [Multi-domain] Cd Length: 98 Bit Score: 72.14 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 23 DGKLLGHVGDEEVLLVQSGDDIFAVGAHCTHYHGPLADGLVVGNSIRCPWHHACFDLRTGEATRAPAFDPIARFKVEQRD 102
Cdd:cd03467 14 GGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSGPAPRPLPKYPVKVEG 93
|
....*
gi 881038642 103 GKVFV 107
Cdd:cd03467 94 DGVVW 98
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
218-396 |
7.20e-15 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 76.71 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 218 DGARLAYDRLLLATGAEPNRLPVPG-ADRPNVHvlrtlaDSNAIIASAKDARRAVVIGASFIGLEAAaSLRAR---DIEV 293
Cdd:PRK07251 113 EKIELTAETIVINTGAVSNVLPIPGlADSKHVY------DSTGIQSLETLPERLGIIGGGNIGLEFA-GLYNKlgsKVTV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 294 HVVGPEKIPMERvlgPEMGRCVRALHEEHGVIFHLE---EGVSAINERGVVLKSGEVIAADLIVSGIGVKPR---LTLAE 367
Cdd:PRK07251 186 LDAASTILPREE---PSVAALAKQYMEEDGITFLLNahtTEVKNDGDQVLVVTEDETYRFDALLYATGRKPNtepLGLEN 262
|
170 180 190
....*....|....*....|....*....|
gi 881038642 368 KAGLTIDRG-VVVDRTLQTSAPGIYAAGDI 396
Cdd:PRK07251 263 TDIELTERGaIKVDDYCQTSVPGVFAVGDV 292
|
|
| Rieske_NirD_small_Bacillus |
cd03530 |
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ... |
30-108 |
1.67e-14 |
|
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar to the Bacillus subtilis small subunit of assimilatory nitrite reductase containing a Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium.
Pssm-ID: 239606 [Multi-domain] Cd Length: 98 Bit Score: 69.17 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 30 VGDEEVLLVQSGDD-IFAVGAHCTHYHGPLADGLVVGNSIRCPWHHACFDLRTGEAtRAPAFDPIARFKVEQRDGKVFVG 108
Cdd:cd03530 20 TGGGEIAVFRTADDeVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEA-QGPDEGCVRTFPVKVEDGRVYLG 98
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
144-438 |
4.20e-13 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 71.72 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 144 LRREQ-FAGEIvmlsseaeaPVDRPNLSKDYLAGSAQADWIPLRSGDFYRDLKIDLRLGV---EADSIDVAGQAVVLKDG 219
Cdd:PRK13748 156 LRRESpFDGGI---------AATVPTIDRSRLLAQQQARVDELRHAKYEGILDGNPAITVlhgEARFKDDQTLIVRLNDG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 220 A--RLAYDRLLLATGAEPNRLPVPG-ADRPnvhvlrtLADSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVV 296
Cdd:PRK13748 227 GerVVAFDRCLIATGASPAVPPIPGlKETP-------YWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTIL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 297 GPEKIPMERvlGPEMGRCVRALHEEHG--VIFHLEEGVSAINERGVVLKS--GEVIAADLIVSgIGVKP---RLTLaEKA 369
Cdd:PRK13748 300 ARSTLFFRE--DPAIGEAVTAAFRAEGieVLEHTQASQVAHVDGEFVLTTghGELRADKLLVA-TGRAPntrSLAL-DAA 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881038642 370 GLTIDRG--VVVDRTLQTSAPGIYAAGDIARWPdrhsgenirveHWV-VAERQGQVVARNMLGAREVFD--AVP 438
Cdd:PRK13748 376 GVTVNAQgaIVIDQGMRTSVPHIYAAGDCTDQP-----------QFVyVAAAAGTRAAINMTGGDAALDltAMP 438
|
|
| PRK09965 |
PRK09965 |
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional |
17-107 |
9.39e-13 |
|
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
Pssm-ID: 170182 [Multi-domain] Cd Length: 106 Bit Score: 64.41 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 17 ELAQFSDGKLLGHVGDEEVLLVQSGDDIFAVGAHCTHYHGPLADGLVVGN-SIRCPWHHACFDLRTGEATRAPAFDPIAR 95
Cdd:PRK09965 8 PVADLPEGEALRVDTSPVIALFNVGGEFYAIDDRCSHGNASLSEGYLEDDaTVECPLHAASFCLRTGKALCLPATDPLRT 87
|
90
....*....|..
gi 881038642 96 FKVEQRDGKVFV 107
Cdd:PRK09965 88 YPVHVEGGDIFI 99
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
216-398 |
2.08e-12 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 69.05 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 216 LKDGarlaYDRLLLATGA-EPNRLPVPGADRPNVH-VLRTLADSNAIIASAKD--ARRAVVIGASFIGLEAA-ASLR--A 288
Cdd:PRK11749 222 LRAG----YDAVFIGTGAgLPRFLGIPGENLGGVYsAVDFLTRVNQAVADYDLpvGKRVVVIGGGNTAMDAArTAKRlgA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 289 RdiEVHVV---GPEkipmervlgpEMGRCVRALH--EEHGVIFHL----------EEGVSAI--------------NERG 339
Cdd:PRK11749 298 E--SVTIVyrrGRE----------EMPASEEEVEhaKEEGVEFEWlaapveilgdEGRVTGVefvrmelgepdasgRRRV 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881038642 340 VVLKSGEVIAADLIVSGIGVKPRLTL---AEKAGLTIDRGVVVD-RTLQTSAPGIYAAGDIAR 398
Cdd:PRK11749 366 PIEGSEFTLPADLVIKAIGQTPNPLIlstTPGLELNRWGTIIADdETGRTSLPGVFAGGDIVT 428
|
|
| Rieske |
pfam00355 |
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ... |
19-97 |
2.17e-12 |
|
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein.
Pssm-ID: 425632 [Multi-domain] Cd Length: 89 Bit Score: 62.75 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 19 AQFSDGKLLGH-VGDEEVLLV-QSGDDIFAVGAHCTHYHGPLADGLVVGNS-IRCPWHHACFDlRTGEATRAPAFDPIAR 95
Cdd:pfam00355 9 SELPEGEPKVVeVGGEPLVVFrDEDGELYALEDRCPHRGAPLSEGKVNGGGrLECPYHGWRFD-GTGKVVKVPAPRPLKS 87
|
..
gi 881038642 96 FK 97
Cdd:pfam00355 88 YP 89
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
226-438 |
4.50e-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: 67.95 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 226 RLLLATGAEPNRLPVPGADRPNVhvlrtlaDSNAIIASAKDARRAVVIGASFIGLEAAASLRA--RDIEVHVvgpEKIPM 303
Cdd:TIGR01438 146 RFLIATGERPRYPGIPGAKELCI-------TSDDLFSLPYCPGKTLVVGASYVALECAGFLAGigLDVTVMV---RSILL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 304 eRVLGPEMGRCVRALHEEHGVIF--HLE-EGVSAINERGVVLKSGEVIAA----DLIVSGIGVKP---RLTLaEKAGLTI 373
Cdd:TIGR01438 216 -RGFDQDCANKVGEHMEEHGVKFkrQFVpIKVEQIEAKVLVEFTDSTNGIeeeyDTVLLAIGRDActrKLNL-ENVGVKI 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881038642 374 DRG---VVVDRTLQTSAPGIYAAGDIArwpdrhsgENiRVEHWVVAERQGQVVARNMLGAREV---FDAVP 438
Cdd:TIGR01438 294 NKKtgkIPADEEEQTNVPYIYAVGDIL--------ED-KPELTPVAIQAGRLLAQRLFKGSTVicdYENVP 355
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
207-438 |
7.24e-12 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 67.26 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 207 IDVAGQavvlkDGARLAYDRLLLATGAEPNRLPVPGADRPNVHvlrtlaDSNAIIASAKDARRAVVIGASFIGLEAAASL 286
Cdd:PRK06327 134 IKVTGE-----DETVITAKHVIIATGSEPRHLPGVPFDNKIIL------DNTGALNFTEVPKKLAVIGAGVIGLELGSVW 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 287 RARDIEVHV--VGPEKIPMErvlGPEMGRCVRALHEEHGVIFHLEEGVSAIN--ERGVVLK------SGEVIAAD-LIVS 355
Cdd:PRK06327 203 RRLGAEVTIleALPAFLAAA---DEQVAKEAAKAFTKQGLDIHLGVKIGEIKtgGKGVSVAytdadgEAQTLEVDkLIVS 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 356 gIGVKPRLT--LAEKAGLTID-RG-VVVDRTLQTSAPGIYAAGDIARWPdrhsgeniRVEHwvVAERQGQVVARNMLGAR 431
Cdd:PRK06327 280 -IGRVPNTDglGLEAVGLKLDeRGfIPVDDHCRTNVPNVYAIGDVVRGP--------MLAH--KAEEEGVAVAERIAGQK 348
|
....*....
gi 881038642 432 EV--FDAVP 438
Cdd:PRK06327 349 GHidYNTIP 357
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
269-345 |
7.26e-12 |
|
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: 61.07 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 269 RAVVIGASFIGLEAAASLRARDIEVHVVGPEKIPMeRVLGPEMGRCVRALHEEHGVIFHLEEGVSAI----NERGVVLKS 344
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIegngDGVVVVLTD 79
|
.
gi 881038642 345 G 345
Cdd:pfam00070 80 G 80
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
222-427 |
1.23e-11 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 66.33 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 222 LAYDRLLLATGAEPNRLPVPGADRpNVHVLRTLADSNAI--------------IASAKDARR---AVVIGASFIGLEAAA 284
Cdd:PTZ00318 112 VPYDKLVVAHGARPNTFNIPGVEE-RAFFLKEVNHARGIrkrivqcieraslpTTSVEERKRllhFVVVGGGPTGVEFAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 285 SLRA--RDiEVHVVGPEKIPMERVLGPEMGRCV-----RALHE-------EHGVIFHLEEGVSAINERGVVLKSGEVIAA 350
Cdd:PTZ00318 191 ELADffRD-DVRNLNPELVEECKVTVLEAGSEVlgsfdQALRKygqrrlrRLGVDIRTKTAVKEVLDKEVVLKDGEVIPT 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 351 DLIVSGIGVKPR-LTLAEKAGLTIDRGVVVDRTLQTS-APGIYAAGDIArwpdrhSGENIRVEHWV-VAERQGQVVARNM 427
Cdd:PTZ00318 270 GLVVWSTGVGPGpLTKQLKVDKTSRGRISVDDHLRVKpIPNVFALGDCA------ANEERPLPTLAqVASQQGVYLAKEF 343
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
196-398 |
1.59e-11 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 66.34 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 196 IDLRLGVEADSiDVAGQAvvLKDgarlAYDRLLLATGAE-PNRLPVPGADRPNVH---------VLRTLADSNAIIASAK 265
Cdd:PRK12810 208 IEFRTNVEVGK-DITAEE--LLA----EYDAVFLGTGAYkPRDLGIPGRDLDGVHfamdfliqnTRRVLGDETEPFISAK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 266 DaRRAVVIGASFIGLEAAA-SLRARDIEVHVVGPEKIPMERVLGPEMGRCVRALHE-----EHGVI---------FHLEE 330
Cdd:PRK12810 281 G-KHVVVIGGGDTGMDCVGtAIRQGAKSVTQRDIMPMPPSRRNKNNPWPYWPMKLEvsnahEEGVErefnvqtkeFEGEN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 331 G-VSAI---------NERGVVLKSGEVIAADLIVSGIG-VKPRLTLAEKAGLTID-RGVVV--DRTLQTSAPGIYAAGDI 396
Cdd:PRK12810 360 GkVTGVkvvrtelgeGDFEPVEGSEFVLPADLVLLAMGfTGPEAGLLAQFGVELDeRGRVAapDNAYQTSNPKVFAAGDM 439
|
..
gi 881038642 397 AR 398
Cdd:PRK12810 440 RR 441
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
227-429 |
2.52e-11 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 65.55 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 227 LLLATGAEPNRLPVPGADRpnvhvlRTLADSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVV--GPEKIPME 304
Cdd:PRK06416 138 IILATGSRPRELPGIEIDG------RVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVeaLPRILPGE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 305 RvlgPEMGRCVRALHEEHGVIFHL----------EEGVSAINERGVVLksgEVIAADLIVSGIGVKPR---LTLaEKAGL 371
Cdd:PRK06416 212 D---KEISKLAERALKKRGIKIKTgakakkveqtDDGVTVTLEDGGKE---ETLEADYVLVAVGRRPNtenLGL-EELGV 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881038642 372 TIDRG-VVVDRTLQTSAPGIYAAGDIARWPdrhsgeniRVEHwvVAERQGQVVARNMLG 429
Cdd:PRK06416 285 KTDRGfIEVDEQLRTNVPNIYAIGDIVGGP--------MLAH--KASAEGIIAAEAIAG 333
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
218-396 |
3.24e-10 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 62.14 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 218 DGARLAY--DRLLLATGAEPNRLPVPGADrpnvhvlrtLADSNAIIASAKD-ARRAVVIGASFIGLEAAASLRARDIEVH 294
Cdd:PLN02507 160 DGTKLRYtaKHILIATGSRAQRPNIPGKE---------LAITSDEALSLEElPKRAVVLGGGYIAVEFASIWRGMGATVD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 295 VVGPEKIPMeRVLGPEMGRCVRALHEEHGVIFHLEEGVSAINERG----VVLKSGEVIAADLIVSGIGVKP---RLTLaE 367
Cdd:PLN02507 231 LFFRKELPL-RGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEggikVITDHGEEFVADVVLFATGRAPntkRLNL-E 308
|
170 180 190
....*....|....*....|....*....|.
gi 881038642 368 KAGLTIDR--GVVVDRTLQTSAPGIYAAGDI 396
Cdd:PLN02507 309 AVGVELDKagAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
192-491 |
5.46e-10 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 61.76 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 192 RDLKIDLRLGVEADSIDVAGQAVVLKDGARLAYDRL-----------LLATGAEPNrLP--VPGADRPNVhvlrtlaDSN 258
Cdd:PTZ00052 102 RSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNsqeetitakyiLIATGGRPS-IPedVPGAKEYSI-------TSD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 259 AIIASAKDARRAVVIGASFIGLEAAASLRARDIEVhVVGPEKIPMeRVLGPEMGRCVRALHEEHGVIFhlEEGVSAIN-- 336
Cdd:PTZ00052 174 DIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDV-TVAVRSIPL-RGFDRQCSEKVVEYMKEQGTLF--LEGVVPINie 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 337 ----ERGVVLKSGEVIAADLIVSGIGVKPrltlaEKAGLTIDR-GVVVDRTLQ-------TSAPGIYAAGDIArwpdrhs 404
Cdd:PTZ00052 250 kmddKIKVLFSDGTTELFDTVLYATGRKP-----DIKGLNLNAiGVHVNKSNKiiapndcTNIPNIFAVGDVV------- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 405 gENiRVEHWVVAERQGQVVARNMLGAREVFDAVPFFWSQHYdIPINY--VGHAEKwDEIVVHGEIMAHDCLLEYklngKT 482
Cdd:PTZ00052 318 -EG-RPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIF-TPIEYgaCGYSSE-AAIAKYGEDDIEEYLQEF----NT 389
|
....*....
gi 881038642 483 LAVASIFRD 491
Cdd:PTZ00052 390 LEIAAVHRE 398
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
218-428 |
7.34e-10 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 61.12 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 218 DGARLAYDRLLLATGAEPNRLPVPGADRPNVHVlrtladSNAIIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVVG 297
Cdd:PRK07846 123 DGEEITADQVVIAAGSRPVIPPVIADSGVRYHT------SDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 298 PEkipmERVLGPEMGRCVRALHEEHGVIF--HLEEGVSAINERG----VVLKSGEVIAADLIVSGIGVKPRLTL--AEKA 369
Cdd:PRK07846 197 RS----GRLLRHLDDDISERFTELASKRWdvRLGRNVVGVSQDGsgvtLRLDDGSTVEADVLLVATGRVPNGDLldAAAA 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881038642 370 GLTIDRG--VVVDRTLQTSAPGIYAAGDIAR-WPDRHsgenirvehwvVAERQGQVVARNML 428
Cdd:PRK07846 273 GVDVDEDgrVVVDEYQRTSAEGVFALGDVSSpYQLKH-----------VANHEARVVQHNLL 323
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
193-401 |
1.02e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 60.90 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 193 DLKIDLRLGVEADSIDVAGQAVVLkDGARLAYDRLLLATGAE-PNRLPVPGADRPNV----HVLRTLADSNAIiasaKDA 267
Cdd:PRK12814 249 DIAPLRAMGAEFRFNTVFGRDITL-EELQKEFDAVLLAVGAQkASKMGIPGEELPGVisgiDFLRNVALGTAL----HPG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 268 RRAVVIGASFIGLEAA-ASLRARDIEVHVV---GPEKIPMERvlgPEMGRcvrALHEehGVIFHL-------EEGVSAIN 336
Cdd:PRK12814 324 KKVVVIGGGNTAIDAArTALRLGAESVTILyrrTREEMPANR---AEIEE---ALAE--GVSLRElaapvsiERSEGGLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 337 ERGVVLKSGE-----------------VIAADLIVSGIGVKPRLTLAEKAGLTIDRG--VVVDR-TLQTSAPGIYAAGDI 396
Cdd:PRK12814 396 LTAIKMQQGEpdesgrrrpvpvegsefTLQADTVISAIGQQVDPPIAEAAGIGTSRNgtVKVDPeTLQTSVAGVFAGGDC 475
|
....*
gi 881038642 397 ARWPD 401
Cdd:PRK12814 476 VTGAD 480
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
202-457 |
5.54e-08 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 55.27 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 202 VEADSIDVagqavvlkDGARLAYDRLLLATGAEPNRLPVPGADrpnvHVLrtlaDSNAIIASAKDARRAVVIGASFIGLE 281
Cdd:PLN02546 203 VDPHTVDV--------DGKLYTARNILIAVGGRPFIPDIPGIE----HAI----DSDAALDLPSKPEKIAIVGGGYIALE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 282 AAASLRARDIEVHVVgpekIPMERVLgpemgrcvRALHEE-----------HGVIFHLEEGVSAI---NERGVVLKS--G 345
Cdd:PLN02546 267 FAGIFNGLKSDVHVF----IRQKKVL--------RGFDEEvrdfvaeqmslRGIEFHTEESPQAIiksADGSLSLKTnkG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 346 EVIAADLIVSGIGVKPR---LTLaEKAGLTIDR--GVVVDRTLQTSAPGIYAAGDIARwpdrhsgeniRVEHWVVAERQG 420
Cdd:PLN02546 335 TVEGFSHVMFATGRKPNtknLGL-EEVGVKMDKngAIEVDEYSRTSVPSIWAVGDVTD----------RINLTPVALMEG 403
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 881038642 421 QVVARNMLG---AREVFDAVP-FFWSQHydiPINYVGHAEK 457
Cdd:PLN02546 404 GALAKTLFGnepTKPDYRAVPsAVFSQP---PIGQVGLTEE 441
|
|
| Rieske_T4moC |
cd03474 |
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ... |
31-110 |
6.86e-08 |
|
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.
Pssm-ID: 239556 [Multi-domain] Cd Length: 108 Bit Score: 50.80 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 31 GDEEVLLVQSGDDIFAVGAHCTHYHGPLADGLVVGNSIRCPWHHACFDLRTGEATrAPAFDPIARFKVEQRDGKVFVGDK 110
Cdd:cd03474 22 GEEVLLVAPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGL-NPRDCRLARYPVKVEGGDILVDTE 100
|
|
| HcaE |
COG4638 |
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ... |
29-113 |
1.29e-06 |
|
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 443676 [Multi-domain] Cd Length: 298 Bit Score: 49.99 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 29 HVGDEEVLLVQSGDD-IFAVGAHCTHYHGPLADGLVVGNSIRCPWHHACFDLrTGEATRAPAFDPIARF----------K 97
Cdd:COG4638 46 TILGEPVVLVRDKDGeVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDL-DGRLVGIPHMEGFPDFdparaglrsvP 124
|
90
....*....|....*...
gi 881038642 98 VEQRDGKVFV--GDKVAP 113
Cdd:COG4638 125 VEEWGGLIFVwlGPDAPP 142
|
|
| Rieske_RO_Alpha_N |
cd03469 |
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ... |
29-107 |
2.79e-06 |
|
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation.
Pssm-ID: 239551 [Multi-domain] Cd Length: 118 Bit Score: 46.43 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 29 HVGDEEVLLVQSGDD-IFAVGAHCTHYHGPLADG-LVVGNSIRCPWHHACFDLrTGEATRAPAFDP----------IARF 96
Cdd:cd03469 20 ELGGEPLVLVRDRDGeVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYDL-DGKLVGVPREEGfpgfdkeklgLRTV 98
|
90
....*....|.
gi 881038642 97 KVEQRDGKVFV 107
Cdd:cd03469 99 PVEEWGGLIFV 109
|
|
| QcrA/PetC |
COG0723 |
Rieske Fe-S protein [Energy production and conversion]; |
1-108 |
4.78e-06 |
|
Rieske Fe-S protein [Energy production and conversion];
Pssm-ID: 440487 [Multi-domain] Cd Length: 118 Bit Score: 45.76 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 1 MQQDDAPKGPDLAGGVELAQFSDGK-LLGHVGDEEVLLVQSG----DDIFAVGAHCTHYHGPLAdGLVVGNSIRCPWHHA 75
Cdd:COG0723 6 FVSPSAKAKAGAPVEVDLSDLPPGEgKVVEWRGKPVFVVRTPvrgdGEIVAVSAICTHLGCPVT-WNADEGGFDCPCHGS 84
|
90 100 110
....*....|....*....|....*....|...
gi 881038642 76 CFDLrTGEATRAPAFDPIARFKVEQRDGKVFVG 108
Cdd:COG0723 85 RFDP-DGRVLKGPAPRPLPVPPLEVDDDKLLIG 116
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
199-398 |
8.45e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 48.09 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 199 RLGVEADSIDVAGQAVVLKD-GARLAYDRLLLATGA-EPNRLPVPG--ADR---PNVHVLRT------LADSNAIIASAK 265
Cdd:PRK12831 203 KLGVKIETNVVVGKTVTIDElLEEEGFDAVFIGSGAgLPKFMGIPGenLNGvfsANEFLTRVnlmkayKPEYDTPIKVGK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 266 darRAVVIGASFIGLEAAASLRARDIEVHVVgpekipmERVLGPEMGRCVRALH--EEHGVIFHL----------EEG-V 332
Cdd:PRK12831 283 ---KVAVVGGGNVAMDAARTALRLGAEVHIV-------YRRSEEELPARVEEVHhaKEEGVIFDLltnpveilgdENGwV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 333 SAIN-------------ERGVVLKSGE--VIAADLIVSGIGVKP-RLTLAEKAGLTIDRG---VVVDRTLQTSAPGIYAA 393
Cdd:PRK12831 353 KGMKcikmelgepdasgRRRPVEIEGSefVLEVDTVIMSLGTSPnPLISSTTKGLKINKRgciVADEETGLTSKEGVFAG 432
|
....*
gi 881038642 394 GDIAR 398
Cdd:PRK12831 433 GDAVT 437
|
|
| nirD_assim_sml |
TIGR02378 |
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ... |
31-108 |
2.38e-05 |
|
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 131431 [Multi-domain] Cd Length: 105 Bit Score: 43.46 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 31 GDEEVLLVQ-SGDDIFAVGAHCTHYHG-PLADGLVVGNS----IRCPWHHACFDLRTGEATRAPAFDpIARFKVEQRDGK 104
Cdd:TIGR02378 22 GDTQIAIFRvPGDQVFAIQNMCPHKRAfVLSRGIVGDAQgelwVACPLHKRNFRLEDGRCLEDDSGS-VRTYEVRVEDGR 100
|
....
gi 881038642 105 VFVG 108
Cdd:TIGR02378 101 VYVA 104
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
199-398 |
3.39e-05 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 46.66 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 199 RLGVEADSIDVAGQAVVLKDGARLAYDRLLLATGAE-PNRLPVPGADRPNVHVLRT-LADSNAIIASAKD-------ARR 269
Cdd:PRK12778 493 KLGVKFETDVIVGKTITIEELEEEGFKGIFIASGAGlPNFMNIPGENSNGVMSSNEyLTRVNLMDAASPDsdtpikfGKK 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 270 AVVIGASFIGLEAA-------------------ASLRARDIEVHVVGPEKI-------PMErVLGPEMGRcVRALHEEhg 323
Cdd:PRK12778 573 VAVVGGGNTAMDSArtakrlgaervtivyrrseEEMPARLEEVKHAKEEGIefltlhnPIE-YLADEKGW-VKQVVLQ-- 648
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881038642 324 vIFHLEEGVSAINERGVVLKSGEV-IAADLIVSGIGVKPR-LTLAEKAGLTIDR--GVVVDRTLQTSAPGIYAAGDIAR 398
Cdd:PRK12778 649 -KMELGEPDASGRRRPVAIPGSTFtVDVDLVIVSVGVSPNpLVPSSIPGLELNRkgTIVVDEEMQSSIPGIYAGGDIVR 726
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
224-401 |
6.23e-05 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 45.64 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 224 YDRLLLATGAE-PNRLPVPGADRPN----VHVLRTLADSNAIiasaKDARRAVVIGASFIGLEAA-ASLRARDIEVHVVg 297
Cdd:PRK12771 223 FDAVFVAIGAQlGKRLPIPGEDAAGvldaVDFLRAVGEGEPP----FLGKRVVVIGGGNTAMDAArTARRLGAEEVTIV- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 298 pEKIPMErvlgpEMGrcvrALHEE------HGVIFHL----------EEGVSAIN----ERGVVLKSG---------EVI 348
Cdd:PRK12771 298 -YRRTRE-----DMP----AHDEEieealrEGVEINWlrtpveiegdENGATGLRvitvEKMELDEDGrpspvtgeeETL 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 881038642 349 AADLIVSGIGVKPRLTLAEKA-GLTIDRGVV-VDRTLQ-TSAPGIYAAGDIARWPD 401
Cdd:PRK12771 368 EADLVVLAIGQDIDSAGLESVpGVEVGRGVVqVDPNFMmTGRPGVFAGGDMVPGPR 423
|
|
| Rieske_2 |
pfam13806 |
Rieske-like [2Fe-2S] domain; |
30-107 |
8.02e-05 |
|
Rieske-like [2Fe-2S] domain;
Pssm-ID: 433491 [Multi-domain] Cd Length: 103 Bit Score: 41.77 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 30 VGDEEV-LLVQSGDDIFAVGAHCT-HYHGPLADGLVV----GNSIRCPWHHACFDLRTGEATRAPAFdPIARFKVEQRDG 103
Cdd:pfam13806 20 VGGRQVaVFRLEDGQVYAIDNRDPfSGANVLSRGIVGdlggELVVASPLYKQHFDLKTGECLEDPEV-SVPVYPVRVRDG 98
|
....
gi 881038642 104 KVFV 107
Cdd:pfam13806 99 NVEV 102
|
|
| Rieske_RO_Alpha_KSH |
cd03531 |
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ... |
21-107 |
8.91e-05 |
|
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase component of 3-ketosteroid 9-alpha-hydroxylase (KSH). The terminal oxygenase component of KSH is a key enzyme in the microbial steroid degradation pathway, catalyzing the 9 alpha-hydroxylation of 4-androstene-3,17-dione (AD) and 1,4-androstadiene-3,17-dione (ADD). KSH is a two-component class IA monooxygenase, with terminal oxygenase (KshA) and oxygenase reductase (KshB) components. KSH activity has been found in many actino- and proteo- bacterial genera including Rhodococcus, Nocardia, Arthrobacter, Mycobacterium, and Burkholderia.
Pssm-ID: 239607 [Multi-domain] Cd Length: 115 Bit Score: 42.02 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 21 FSDGK--LLGHVGDEEVLLVQSGDDIFAVGAHCTHYHGPLADGLVVGNSIRCPWHhacfDLRTG---------EATRAPA 89
Cdd:cd03531 11 FRDGKphGVEAFGTKLVVFADSDGALNVLDAYCRHMGGDLSQGTVKGDEIACPFH----DWRWGgdgrckaipYARRVPP 86
|
90
....*....|....*...
gi 881038642 90 FDPIARFKVEQRDGKVFV 107
Cdd:cd03531 87 LARTRAWPTLERNGQLFV 104
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
185-396 |
2.42e-04 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 43.46 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 185 LRSGDFYR--DL-KIDLRLGvEADSIDVAGQAVVLKDGAR-LAYDRLLLATGAEPNRLPVPG-ADRPNVHvlrtlaDSNA 259
Cdd:PRK08010 78 LRNKNFHNlaDMpNIDVIDG-QAEFINNHSLRVHRPEGNLeIHGEKIFINTGAQTVVPPIPGiTTTPGVY------DSTG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 260 IIASAKDARRAVVIGASFIGLEAAASLRARDIEVHVV--GPEKIPME-RVLGPEMGRCVRalheEHGVIFHLEEGVSAIN 336
Cdd:PRK08010 151 LLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeaASLFLPREdRDIADNIATILR----DQGVDIILNAHVERIS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881038642 337 --ERGVVLKSGE-VIAADLIVSGIGVKPRLT--LAEKAGLTIDR--GVVVDRTLQTSAPGIYAAGDI 396
Cdd:PRK08010 227 hhENQVQVHSEHaQLAVDALLIASGRQPATAslHPENAGIAVNErgAIVVDKYLHTTADNIWAMGDV 293
|
|
| Rieske_RO_Alpha_VanA_DdmC |
cd03532 |
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ... |
32-109 |
3.06e-04 |
|
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and dicamba O-demethylase oxygenase (DdmC) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Vanillate-O-demethylase is a heterodimeric enzyme consisting of a terminal oxygenase (VanA) and reductase (VanB) components. This enzyme reductively catalyzes the conversion of vanillate into protocatechuate and formaldehyde. Protocatechuate and vanillate are important intermediate metabolites in the degradation pathway of lignin-derived compounds such as ferulic acid and vanillin by soil microbes. DDmC is the oxygenase component of a three-component dicamba O-demethylase found in Pseudomonas maltophila, that catalyzes the conversion of a widely used herbicide called herbicide dicamba (2-methoxy-3,6-dichlorobenzoic acid) to DCSA (3,6-dichlorosalicylic acid).
Pssm-ID: 239608 [Multi-domain] Cd Length: 116 Bit Score: 40.43 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 32 DEEVLLVQSGD-DIFAVGAHCTHYHGPLADGLVVGNSIRCPWHHACFDlRTGEAT------RAPAFDPIARFKVEQRDGK 104
Cdd:cd03532 26 GEPVVLYRTQDgRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFD-SDGRCVhmpgqeRVPAKACVRSYPVVERDAL 104
|
....*..
gi 881038642 105 VFV--GD 109
Cdd:cd03532 105 IWIwmGD 111
|
|
| Rieske_RO_Alpha_PrnD |
cd03537 |
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ... |
50-118 |
3.48e-04 |
|
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of aminopyrrolnitrin oxygenase (PrnD). PrnD is a novel Rieske N-oxygenase that catalyzes the final step in the pyrrolnitrin biosynthetic pathway, the oxidation of the amino group in aminopyrrolnitrin to a nitro group, forming the antibiotic pyrrolnitrin. The biosynthesis of pyrrolnitrin is one of the best examples of enzyme-catalyzed arylamine oxidation. Although arylamine oxygenases are widely distributed within the microbial world and used in a variety of metabolic reactions, PrnD represents one of only two known examples of arylamine oxygenases or N-oxygenases involved in arylnitro group formation, the other being AurF involved in aureothin biosynthesis.
Pssm-ID: 239611 [Multi-domain] Cd Length: 123 Bit Score: 40.30 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 50 HCTHYHGPLADGLVVGNSIRCPWHH-------ACFDLrTGEATRAPAFDPIAR------FKVEQRDGKVFV--GdkvAPC 114
Cdd:cd03537 43 HCSHLGANLADGRVKDGCIQCPFHHwrydeqgQCVHI-PGHSTAVRRLEPVPRgarqptLVTAERYGYVWVwyG---SPQ 118
|
....
gi 881038642 115 PIRP 118
Cdd:cd03537 119 PLHP 122
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
367-395 |
4.79e-04 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 42.54 E-value: 4.79e-04
10 20 30
....*....|....*....|....*....|.
gi 881038642 367 EKAGLTIDRG--VVVDRTLQTSAPGIYAAGD 395
Cdd:PRK07845 282 EEAGVELTPSghITVDRVSRTSVPGIYAAGD 312
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
267-386 |
5.70e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 39.09 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 267 ARRAVVIGASFIGLEAAASLRARDIEVHVVgpEKIPMERVLGPEM---GRCVRALHE--------EHGVIFhleEGVSAI 335
Cdd:PRK06847 4 VKKVLIVGGGIGGLSAAIALRRAGIAVDLV--EIDPEWRVYGAGItlqGNALRALRElgvldeclEAGFGF---DGVDLF 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881038642 336 NERGVVLKS--GEVIAADLIVSGIGVkPRLTL-------AEKAGLTIDRGVVVDRTLQTS 386
Cdd:PRK06847 79 DPDGTLLAElpTPRLAGDDLPGGGGI-MRPALariladaARAAGADVRLGTTVTAIEQDD 137
|
|
| Reductase_C |
pfam14759 |
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ... |
440-507 |
8.11e-03 |
|
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerization. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).
Pssm-ID: 434185 [Multi-domain] Cd Length: 83 Bit Score: 35.62 E-value: 8.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881038642 440 FWSQHYDIPINYVGHAEKWDEIVVHGEIMAHDCLLEYKLNGKTLAVASIFRDADSLKAAAAMEEGRAP 507
Cdd:pfam14759 2 FWSDQYDLKLQIAGLPTGADEVVLRGDPEDGAFSVFYLRDGRLVAVDAVNRPRDFMAARRLIARGASV 69
|
|
| |
