|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
194-562 |
9.74e-105 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 322.09 E-value: 9.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSL--DTQPEQLALRPKEFFRAYGIEVLTEAQVV 271
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLagETDEEDLLLRPADFYEENGIDLRLGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 272 TVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVV-RLARGRNVVVVGAGFLGMEVAAY 350
Cdd:COG1251 81 AIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRaALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 351 LTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGqEGKLKEVVLKSSKVVRADVCVVGIGAV 430
Cdd:COG1251 161 LRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 431 PATGFLRQSGIGLDsRGfIPVNKMMQTNVPGVFAAGDAVTFPLAWRNNRKVniPHWQMAHAQGRVAAQNMLAQEAEMS-T 509
Cdd:COG1251 240 PNTELARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVL--ELVAPAYEQARVAAANLAGGPAAYEgS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1900245201 510 VPYLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMN 562
Cdd:COG1251 316 VPSTKLKVFGVDVASAGDAEGDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVG 368
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
215-530 |
4.07e-84 |
|
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: 265.91 E-value: 4.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 215 QEGFSDRIVLctLDR--HLPYDRPKLSKSL---DTQPEQLALRPKEFFRAYGIEVLTEAQVVTVDVRTKKVVFKDGFKLE 289
Cdd:COG0446 1 RLGPDAEITV--IEKgpHHSYQPCGLPYYVgggIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 290 YSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRV---VRLARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEET 366
Cdd:COG0446 79 YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALreaLKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 367 PFRRFLGErVGRALMKMFENNRVKFYMQTEVSELRGQEGklKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIGLDSR 446
Cdd:COG0446 159 LLGVLDPE-MAALLEEELREHGVELRLGETVVAIDGDDK--VAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 447 GFIPVNKMMQTNVPGVFAAGDAVTFPLAwRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEMSTVPYLWTAMFGksLRYAG 526
Cdd:COG0446 236 GWIKVDETLQTSDPDVYAAGDCAEVPHP-VTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFD--LCIAS 312
|
....
gi 1900245201 527 YGEG 530
Cdd:COG0446 313 TGTG 316
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
195-493 |
3.35e-73 |
|
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: 236.83 E-value: 3.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 195 TNVLIVGAGAAGLVCAETLRQEGFsdRIVLCTLDRHLPYDRPKLSKSLD---------TQPEQLALRPKEFFRAY--GIE 263
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGG--KVTLIEDEGTCPYGGCVLSKALLgaaeapeiaSLWADLYKRKEEVVKKLnnGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 264 VLTEAQVVTVDVRTKKVVFK-----DGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARGRNVVVV 338
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKRVVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 339 GAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLkEVVLKSSKVV 418
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGV-EVILKDGTEI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1900245201 419 RADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAvtfplawrnnRKVNIPHWQMAHAQG 493
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC----------RVGGPELAQNAVAQG 301
|
|
| Rieske_AIFL_N |
cd03478 |
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ... |
70-164 |
2.55e-55 |
|
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: 182.05 E-value: 2.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 70 AAVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03478 1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
|
90
....*....|....*
gi 1900245201 150 SLHKFQVKIEKEKVY 164
Cdd:cd03478 81 SLPCYEVEVEDGRVY 95
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
194-585 |
7.04e-55 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 191.29 E-value: 7.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSLDTQPEQL--ALRPKEFFRAYGIEVLTEAQVV 271
Cdd:PRK09754 3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQlqQVLPANWWQENNVHLHSGVTIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 272 TVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVR-LARGRNVVVVGAGFLGMEVAAY 350
Cdd:PRK09754 83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREvLQPERSVVIVGAGTIGLELAAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 351 LTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELrgQEGKLKEVVLKSSKVVRADVCVVGIGAV 430
Cdd:PRK09754 163 ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV--VDGEKVELTLQSGETLQADVVIYGIGIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 431 PATGFLRQSgiGLDSRGFIPVNKMMQTNVPGVFAAGDAVT--FPLAWRNNRKVniphWQMAHAQGRVAAQNMLAQEAEMS 508
Cdd:PRK09754 241 ANDQLAREA--NLDTANGIVIDEACRTCDPAIFAGGDVAItrLDNGALHRCES----WENANNQAQIAAAAMLGLPLPLL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1900245201 509 TVPYLWTAMFGKSLRYAGYGEGfDDVIIQGDLEELKFVAFYTKGDEVIAVASMNYDPIVSKVAEVLASGRAIRKREV 585
Cdd:PRK09754 315 PPPWFWSDQYSDNLQFIGDMRG-DDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLL 390
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
195-512 |
5.01e-41 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 152.98 E-value: 5.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 195 TNVLIVGAGAAGLVCAETLRQEGFSD-RIVLctLDR--HLPYdRPKL----SKSLDtqPEQLALRPKEFFRAYGIEVLTe 267
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDaEVTL--IDPnpYHLF-QPLLpevaAGTLS--PDDIAIPLRELLRRAGVRFIQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 268 AQVVTVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEvENVFTIRTPEDA----NRVVRL------ARGRNVVV 337
Cdd:COG1252 76 GEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDAlalrERLLAAferaerRRLLTIVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 338 VGAGFLGMEVAAYLTEKAH-------------SVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGqe 404
Cdd:COG1252 155 VGGGPTGVELAGELAELLRkllrypgidpdkvRITLVEAGPRILPGL-GEKLSEAAEKELEKRGVEVHTGTRVTEVDA-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 405 gklKEVVLKSSKVVRADvCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQT-NVPGVFAAGDAVTFPLAwrnnrkvnI 483
Cdd:COG1252 232 ---DGVTLEDGEEIPAD-TVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDP--------D 299
|
330 340 350
....*....|....*....|....*....|....
gi 1900245201 484 PHW-----QMAHAQGRVAAQNMLAQEAEMSTVPY 512
Cdd:COG1252 300 GKPvpktaQAAVQQAKVLAKNIAALLRGKPLKPF 333
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
195-499 |
6.44e-38 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 142.18 E-value: 6.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 195 TNVLIVGAGAAGLVCAETLRQEGFSdrIVLctLDRHLP----------YDRPKLSKSLdtQPEQLALRPKEFFRAYGIEV 264
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLK--TLV--IEGGEPggqlattkeiENYPGFPEGI--SGPELAERLREQAERFGAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 265 LTEaQVVTVDV--RTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGkevENVFTIR-----TPEDANrvvrLARGRNVVV 337
Cdd:COG0492 75 LLE-EVTSVDKddGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPG---EEEFEGRgvsycATCDGF----FFRGKDVVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 338 VGAGFLGMEVAAYLTEKAHSVSVVeleetpFRR--FLGERVgrALMKMFENNRVKFYMQTEVSELRGqEGKLKEVVLKSS 415
Cdd:COG0492 147 VGGGDSALEEALYLTKFASKVTLI------HRRdeLRASKI--LVERLRANPKIEVLWNTEVTEIEG-DGRVEGVTLKNV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 416 K-----VVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFplawrnnrkvniPHWQMAH 490
Cdd:COG0492 218 KtgeekELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY------------KYRQAAT 285
|
330
....*....|.
gi 1900245201 491 A--QGRVAAQN 499
Cdd:COG0492 286 AagEGAIAALS 296
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
195-490 |
8.96e-35 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 136.84 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 195 TNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRH-------LPYdrpKLSKSLDTQPEQLALRPKEFFRAYGIEVLTE 267
Cdd:PRK13512 2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDmsfancaLPY---YIGEVVEDRKYALAYTPEKFYDRKQITVKTY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 268 AQVVTVDVRTKKVVFKD-----GFKLEYSKLLLAPGSSPKTLsckGKEVENVFTIRTPEDANRV---VRLARGRNVVVVG 339
Cdd:PRK13512 79 HEVIAINDERQTVTVLNrktneQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIdqfIKANQVDKALVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 340 AGFLGMEVAAYLTEKAHSVSVVElEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEgklkeVVLKSSKVVR 419
Cdd:PRK13512 156 AGYISLEVLENLYERGLHPTLIH-RSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNE-----VTFKSGKVEH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 420 ADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVT-----------FPLAWRNNRKVNIPHWQM 488
Cdd:PRK13512 230 YDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITshyrhvdlpasVPLAWGAHRAASIVAEQI 309
|
..
gi 1900245201 489 AH 490
Cdd:PRK13512 310 AG 311
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
197-508 |
4.66e-33 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 132.09 E-value: 4.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFSDRIVL-----------CTLdrhlPYdrpKLSKSLDtQPEQLALRPKEFFRAYGIEVL 265
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNKELEITVyektdivsfgaCGL----PY---FVGGFFD-DPNTMIARTPEEFIKSGIDVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 266 TEAQVVTVDVRTKKVVFKDG-----FKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARG---RNVVV 337
Cdd:PRK09564 75 TEHEVVKVDAKNKTITVKNLktgsiFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDeeiKNIVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 338 VGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFLGERVGRALMKMFEN----NRVKFYMQTEVSELRGqEGKLKEVVLK 413
Cdd:PRK09564 155 IGAGFIGLEAVEAAKHLGKNVRIIQLED----RILPDSFDKEITDVMEEelreNGVELHLNEFVKSLIG-EDKVEGVVTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 414 SSKVVrADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD-AVTFPLAwrNNRKVNIPHWQMAHAQ 492
Cdd:PRK09564 230 KGEYE-ADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcATIYNIV--SNKNVYVPLATTANKL 306
|
330
....*....|....*.
gi 1900245201 493 GRVAAQNMLAQEAEMS 508
Cdd:PRK09564 307 GRMVGENLAGRHVSFK 322
|
|
| NirD |
COG2146 |
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ... |
69-166 |
1.74e-29 |
|
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: 112.24 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 69 EAAVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGL 148
Cdd:COG2146 3 EVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLGGPAT 82
|
90
....*....|....*...
gi 1900245201 149 DSLHKFQVKIEKEKVYVR 166
Cdd:COG2146 83 EPLKTYPVRVEDGDVYVD 100
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
197-512 |
5.14e-29 |
|
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: 120.19 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFsdRIVL---------CTLD------------------RHLP----------YDRPKLS 239
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGL--KVALvekgrlggtCLNVgcipskallhaaevaheaRHAAefgisagapsVDWAALM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 240 KSLDTQPEQLALRPKEFFRAYGIEVLT-EAQVV---TVDVRTKKVvfkdgfkLEYSKLLLAPGSSPKTLSCKGKEVENVF 315
Cdd:COG1249 84 ARKDKVVDRLRGGVEELLKKNGVDVIRgRARFVdphTVEVTGGET-------LTADHIVIATGSRPRVPPIPGLDEVRVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 316 TIRTpedanrVVRLAR-GRNVVVVGAGFLGMEVAAYL----TEkahsVSVVELEETPFRRFlGERVGRALMKMFENNRVK 390
Cdd:COG1249 157 TSDE------ALELEElPKSLVVIGGGYIGLEFAQIFarlgSE----VTLVERGDRLLPGE-DPEISEALEKALEKEGID 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 391 FYMQTEVSELRGQEGKLKeVVLKS---SKVVRADVCVVGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNVPGVFAA 465
Cdd:COG1249 226 ILTGAKVTSVEKTGDGVT-VTLEDgggEEAVEADKVLVATGRRPNTDglGLEAAGVELDERGGIKVDEYLRTSVPGIYAI 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1900245201 466 GDAVTFP-LAwrnnrkvnipHwqMAHAQGRVAAQNMLAQEAE---MSTVPY 512
Cdd:COG1249 305 GDVTGGPqLA----------H--VASAEGRVAAENILGKKPRpvdYRAIPS 343
|
|
| Rieske |
cd03467 |
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ... |
71-165 |
3.28e-22 |
|
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: 91.40 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 71 AVCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03467 3 VVGALSELPPGGGRVVVVGGGPVVVVrREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSGPAPR 82
|
90
....*....|....*.
gi 1900245201 150 SLHKFQVKIEKEKVYV 165
Cdd:cd03467 83 PLPKYPVKVEGDGVVW 98
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
193-508 |
1.20e-21 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 99.81 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 193 SSTNVLIVGAGAAGLVCAETLRQEGFSDRI---VLCTLDRhLPYDRPKLSKSLDTQ-PEQLALRPKEFFRAYGIEVLTEA 268
Cdd:PRK14989 2 SKVRLAIIGNGMVGHRFIEDLLDKADAANFditVFCEEPR-IAYDRVHLSSYFSHHtAEELSLVREGFYEKHGIKVLVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 269 QVVTVDvRTKKVVFKD-GFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLA-RGRNVVVVGAGFLGME 346
Cdd:PRK14989 81 RAITIN-RQEKVIHSSaGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACArRSKRGAVVGGGLLGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 347 VAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSEL--RGQEGKlKEVVLKSSKVVRADVCV 424
Cdd:PRK14989 160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIvqEGVEAR-KTMRFADGSELEVDFIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 425 VGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVtfplAWrNNRKVNI--PHWQMAhaqgRVAAQNMLA 502
Cdd:PRK14989 239 FSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECA----SW-NNRVFGLvaPGYKMA----QVAVDHLLG 309
|
330
....*....|.
gi 1900245201 503 QE-----AEMS 508
Cdd:PRK14989 310 SEnafegADLS 320
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
197-502 |
1.84e-21 |
|
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: 97.13 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFSdrivlCTL-DRHlpyDRP-----------KLSKSLdtqpeqlALRPKEFFRAYGIEV 264
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHE-----VTVfEAL---DKPggllrygipefRLPKDV-------LDREIELIEALGVEF 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 265 LTEAQV-VTVDVrtkkvvfkDGFKLEYSKLLLAPGSS-PKTLSCKGKEVENVFT----IRtpeDANRVV----RLARGRN 334
Cdd:COG0493 189 RTNVEVgKDITL--------DELLEEFDAVFLATGAGkPRDLGIPGEDLKGVHSamdfLT---AVNLGEapdtILAVGKR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 335 VVVVGAGFLGMEVA--AyLTEKAHSVSVVEL---EETPFRRflgERVGRALMkmfENNRVKFYMQTEvsELRGQE-GKLK 408
Cdd:COG0493 258 VVVIGGGNTAMDCArtA-LRLGAESVTIVYRrtrEEMPASK---EEVEEALE---EGVEFLFLVAPV--EIIGDEnGRVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 409 EVVLK--------------------SSKVVRADVCVVGIGAVPATGFLR-QSGIGLDSRGFIPVNKM-MQTNVPGVFAAG 466
Cdd:COG0493 329 GLECVrmelgepdesgrrrpvpiegSEFTLPADLVILAIGQTPDPSGLEeELGLELDKRGTIVVDEEtYQTSLPGVFAGG 408
|
330 340 350
....*....|....*....|....*....|....*...
gi 1900245201 467 DAVTFP--LAWrnnrkvniphwqmAHAQGRVAAQNMLA 502
Cdd:COG0493 409 DAVRGPslVVW-------------AIAEGRKAARAIDR 433
|
|
| Rieske |
pfam00355 |
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ... |
72-154 |
2.12e-20 |
|
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: 85.86 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 72 VCHVKDLENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFNIsTGDLEDFPGLD 149
Cdd:pfam00355 5 VCHSSELPEGEPKVVEVGGEPLVVFRDeDGELYALEDRCPHRGAPLSEGkVNGGGRLECPYHGWRFDG-TGKVVKVPAPR 83
|
....*
gi 1900245201 150 SLHKF 154
Cdd:pfam00355 84 PLKSY 88
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
273-512 |
1.72e-19 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 91.37 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 273 VDVRTKKVVFKDGFKLEYS--KLLLAPGSSPKtlscKGKEVEnvFTIRTPEDANRVVRLAR-GRNVVVVGAGFLGMEVAA 349
Cdd:PRK05249 119 VDPHTVEVECPDGEVETLTadKIVIATGSRPY----RPPDVD--FDHPRIYDSDSILSLDHlPRSLIIYGAGVIGCEYAS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 350 YLTEKAHSVSVVELEETPFRrFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKlKEVVLKSSKVVRADVCVVGIGA 429
Cdd:PRK05249 193 IFAALGVKVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG-VIVHLKSGKKIKADCLLYANGR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 430 VPATGFLRQSGIGL--DSRGFIPVNKMMQTNVPGVFAAGDAVTFP-LAwrnnrkvniphwQMAHAQGRVAAQNMLAQEAE 506
Cdd:PRK05249 271 TGNTDGLNLENAGLeaDSRGQLKVNENYQTAVPHIYAVGDVIGFPsLA------------SASMDQGRIAAQHAVGEATA 338
|
....*...
gi 1900245201 507 M--STVPY 512
Cdd:PRK05249 339 HliEDIPT 346
|
|
| Rieske_RO_ferredoxin |
cd03528 |
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ... |
72-166 |
5.82e-19 |
|
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: 82.15 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 72 VCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLDSL 151
Cdd:cd03528 4 VCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPATEPL 83
|
90
....*....|....*
gi 1900245201 152 HKFQVKIEKEKVYVR 166
Cdd:cd03528 84 KTYPVKVEDGDVYVD 98
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
194-513 |
1.16e-18 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 88.05 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSK--SLDTQPEQLA-LRPKEFFRAYGIEVLTEAQV 270
Cdd:PRK04965 2 SNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHvfSQGQRADDLTrQSAGEFAEQFNLRLFPHTWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 271 VTVDVRTKKVVFKDGfKLEYSKLLLAPGSSPKTLSCKGKEVenVFTI------RTPEDanrvvRLARGRNVVVVGAGFLG 344
Cdd:PRK04965 82 TDIDAEAQVVKSQGN-QWQYDKLVLATGASAFVPPIPGREL--MLTLnsqqeyRAAET-----QLRDAQRVLVVGGGLIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 345 MEVAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKeVVLKSSKVVRADVCV 424
Cdd:PRK04965 154 TELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR-ATLDSGRSIEVDAVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 425 VGIGAVPATGFLRQSGIGLDsRGfIPVNKMMQTNVPGVFAAGDAVTFplawrnNRKVnIPHWQMAHAQGRVAAQNMLAQE 504
Cdd:PRK04965 233 AAAGLRPNTALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGDCAEI------NGQV-LPFLQPIQLSAMALAKNLLGQN 303
|
....*....
gi 1900245201 505 AEMSTVPYL 513
Cdd:PRK04965 304 TPLKLPAML 312
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
197-469 |
6.92e-18 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 86.76 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFS----DRivlctldrhlpYDRP-----------KLSKSL-DTQPEQLalrpkeffRAY 260
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKvtvfER-----------ADRIggllrygipdfKLEKEViDRRIELM--------EAE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 261 GIEVLTEAQV-VTVDVrtkkvvfkDGFKLEYSKLLLAPGSS-PKTLSCKGKEVENV-----FTIrtpeDANRVVR----- 328
Cdd:PRK12810 207 GIEFRTNVEVgKDITA--------EELLAEYDAVFLGTGAYkPRDLGIPGRDLDGVhfamdFLI----QNTRRVLgdete 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 329 ---LARGRNVVVVGAGFLGME-VAAYLTEKAhsVSVVELEET---PFRRFLGERVGRALMKMfennRVK----------F 391
Cdd:PRK12810 275 pfiSAKGKHVVVIGGGDTGMDcVGTAIRQGA--KSVTQRDIMpmpPSRRNKNNPWPYWPMKL----EVSnaheegvereF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 392 YMQTEvsELRGQEGKLKEV--------------VLKSSKVVRADVCVVGIGAVPA-TGFLRQSGIGLDSRGFIPVNKM-M 455
Cdd:PRK12810 349 NVQTK--EFEGENGKVTGVkvvrtelgegdfepVEGSEFVLPADLVLLAMGFTGPeAGLLAQFGVELDERGRVAAPDNaY 426
|
330
....*....|....
gi 1900245201 456 QTNVPGVFAAGDAV 469
Cdd:PRK12810 427 QTSNPKVFAAGDMR 440
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
257-507 |
1.14e-17 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 85.97 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 257 FRAYGIEVLT-EAQVV---TVDVRTKKV----VFKDgfkleyskLLLAPGSSPKTLscKGKEVENVfTIRTPEDANRVVR 328
Cdd:PRK06416 102 LKKNKVDIIRgEAKLVdpnTVRVMTEDGeqtyTAKN--------IILATGSRPREL--PGIEIDGR-VIWTSDEALNLDE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 329 LARgrNVVVVGAGFLGMEVA-AYLTEKAHsVSVVELEEtpfrRFLG---ERVGRALMKMFENNRVKFYMQTEVSEL-RGQ 403
Cdd:PRK06416 171 VPK--SLVVIGGGYIGVEFAsAYASLGAE-VTIVEALP----RILPgedKEISKLAERALKKRGIKIKTGAKAKKVeQTD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 404 EG-KLKEVVLKSSKVVRADVCVVGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTNVPGVFAAGDAVTFPlawr 476
Cdd:PRK06416 244 DGvTVTLEDGGKEETLEADYVLVAVGRRPNT-----ENLGLEElgvktdRGFIEVDEQLRTNVPNIYAIGDIVGGP---- 314
|
250 260 270
....*....|....*....|....*....|....
gi 1900245201 477 nnrkvniphwQMAH---AQGRVAAQNMLAQEAEM 507
Cdd:PRK06416 315 ----------MLAHkasAEGIIAAEAIAGNPHPI 338
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
333-506 |
3.23e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 81.38 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 333 RNVVVVGAGFLGMEVAAYLtekaHS----VSVVELEEtpfrRFLG---ERVGRALMKMFENnRVKFYMQTEVSELRgQEG 405
Cdd:PRK06292 170 KSLAVIGGGVIGLELGQAL----SRlgvkVTVFERGD----RILPledPEVSKQAQKILSK-EFKIKLGAKVTSVE-KSG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 406 KLKEVVLKS---SKVVRADVCVVGIGAVPAT---GfLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPLawrnnr 479
Cdd:PRK06292 240 DEKVEELEKggkTETIEADYVLVATGRRPNTdglG-LENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPP------ 312
|
170 180 190
....*....|....*....|....*....|
gi 1900245201 480 kvniphwqMAHA---QGRVAAQNMLAQEAE 506
Cdd:PRK06292 313 --------LLHEaadEGRIAAENAAGDVAG 334
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
197-470 |
6.09e-16 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 80.61 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFSdriVlcTL-DRHlpyDRP-----------KLSKSLdtqpeqlALRPKEFFRAYGIEV 264
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYD---V--TIfEAR---DKAggllrygipefRLPKDI-------VDREVERLLKLGVEI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 265 LTEAQV---VTVDvrtkkvvfkdGFKLEYSKLLLAPG-SSPKTLSCKGKEVENVFT----IRTPEDANRVVRLARGRNVV 336
Cdd:PRK11749 208 RTNTEVgrdITLD----------ELRAGYDAVFIGTGaGLPRFLGIPGENLGGVYSavdfLTRVNQAVADYDLPVGKRVV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 337 VVGAGFLGMEVAAylTEK---AHSVSVV---ELEETP---------------FR------RFLGERVGRALMKmfennrv 389
Cdd:PRK11749 278 VIGGGNTAMDAAR--TAKrlgAESVTIVyrrGREEMPaseeevehakeegveFEwlaapvEILGDEGRVTGVE------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 390 kfYMQTEVSELRGQeGKLKEVVLKSSKVVRADVCVVGIGAVPATGFLR-QSGIGLDSRG-FIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK11749 349 --FVRMELGEPDAS-GRRRVPIEGSEFTLPADLVIKAIGQTPNPLILStTPGLELNRWGtIIADDETGRTSLPGVFAGGD 425
|
...
gi 1900245201 468 AVT 470
Cdd:PRK11749 426 IVT 428
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
197-522 |
4.76e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 78.04 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFSdriVLCTLDRHLPYDRPKL-----------SKSLDTQPEQLAlRPKEFFRAYGIEVl 265
Cdd:PRK06327 7 VVVIGAGPGGYVAAIRAAQLGLK---VACIEAWKNPKGKPALggtclnvgcipSKALLASSEEFE-NAGHHFADHGIHV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 266 teaQVVTVDV-----RTKKVV--FKDG----FK--------------------------------LEYSKLLLAPGSSPK 302
Cdd:PRK06327 82 ---DGVKIDVakmiaRKDKVVkkMTGGieglFKknkitvlkgrgsfvgktdagyeikvtgedetvITAKHVIIATGSEPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 303 TLSckgkevenvftiRTPEDANRVV-------------RLArgrnvvVVGAGFLGMEVAAYLTEKAHSVSVveLEETPfr 369
Cdd:PRK06327 159 HLP------------GVPFDNKIILdntgalnftevpkKLA------VIGAGVIGLELGSVWRRLGAEVTI--LEALP-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 370 RFLG---ERVGRALMKMFENNRVKFYMQTEVSELRGQEgklKEVVLK------SSKVVRADVCVVGIGAVPATGFLRQSG 440
Cdd:PRK06327 217 AFLAaadEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGG---KGVSVAytdadgEAQTLEVDKLIVSIGRVPNTDGLGLEA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 441 IGL--DSRGFIPVNKMMQTNVPGVFAAGDAVtfplawrnnRKvniphWQMAHA---QGRVAAQNMLAQEAEM--STVPY- 512
Cdd:PRK06327 294 VGLklDERGFIPVDDHCRTNVPNVYAIGDVV---------RG-----PMLAHKaeeEGVAVAERIAGQKGHIdyNTIPWv 359
|
410
....*....|....
gi 1900245201 513 LWT----AMFGKSL 522
Cdd:PRK06327 360 IYTspeiAWVGKTE 373
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
245-500 |
6.91e-14 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 74.03 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 245 QPeQLALRPKEFFRAYGIEVLTEAQVVTVDVRTKKV-VFKDGFKLEYSKLLLAPGSSPKTLSCKG--------KEVENVF 315
Cdd:PTZ00318 69 RP-ALAKLPNRYLRAVVYDVDFEEKRVKCGVVSKSNnANVNTFSVPYDKLVVAHGARPNTFNIPGveerafflKEVNHAR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 316 TIR---------------TPEDANRVVrlargrNVVVVGAGFLGMEVAAYLTE--------------KAHSVSVVELEET 366
Cdd:PTZ00318 148 GIRkrivqcieraslpttSVEERKRLL------HFVVVGGGPTGVEFAAELADffrddvrnlnpelvEECKVTVLEAGSE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 367 PFRRFlGERVGRALMKMFENNRVKFYMQTEVSELrgqegKLKEVVLKSSKVVRADVCV--VGIGAVPATgflRQSGIGLD 444
Cdd:PTZ00318 222 VLGSF-DQALRKYGQRRLRRLGVDIRTKTAVKEV-----LDKEVVLKDGEVIPTGLVVwsTGVGPGPLT---KQLKVDKT 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1900245201 445 SRGFIPVNKMMQT-NVPGVFAAGDAVTfplawrNNRKVNIPHWQMAHAQGRVAAQNM 500
Cdd:PTZ00318 293 SRGRISVDDHLRVkPIPNVFALGDCAA------NEERPLPTLAQVASQQGVYLAKEF 343
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
249-468 |
5.65e-13 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 71.39 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 249 LALRPKEFFRAYGI--EVLTEAQVV-------TVDVRTKKVVFKDGFKLEYS--KLLLAPGSSPKTLSCKGKEVEnvfti 317
Cdd:PLN02507 116 LQKKTDEILRLNGIykRLLANAGVKlyegegkIVGPNEVEVTQLDGTKLRYTakHILIATGSRAQRPNIPGKELA----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 318 RTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERvgRALM-KMFENNRVKFYMQTE 396
Cdd:PLN02507 191 ITSDEALSLEELPK--RAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEM--RAVVaRNLEGRGINLHPRTN 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900245201 397 VSELRGQEGKLKeVVLKSSKVVRADVCVVGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDA 468
Cdd:PLN02507 267 LTQLTKTEGGIK-VITDHGEEFVADVVLFATGRAPNTKRlnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
334-411 |
1.02e-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: 63.76 E-value: 1.02e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1900245201 334 NVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPfRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVV 411
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL-LPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
197-472 |
2.63e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 68.48 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpYDRpklsksldtQPEQLAL--------R-PKEFFRAyGIEVLTE 267
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGYEVHV----------YDK---------LPEPGGLmlfgipefRiPIERVRE-GVKELEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 268 AQVVTVdVRTK------------------KVVFKDGFKlEYSKLLLAPGS-SPKTLSCKGKEVENV-------FTIRTPE 321
Cdd:PRK12770 81 AGVVFH-TRTKvccgeplheeegdefverIVSLEELVK-KYDAVLIATGTwKSRKLGIPGEDLPGVysaleylFRIRAAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 322 DA---NRVVRLARGRNVVVVGAGFLGMEVA--AYLtEKAHSVSVV---ELEETPFRRFLGERVGRALMKMFEN-NRVKFY 392
Cdd:PRK12770 159 LGylpWEKVPPVEGKKVVVVGAGLTAVDAAleAVL-LGAEKVYLAyrrTINEAPAGKYEIERLIARGVEFLELvTPVRII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 393 MQTEVSELRGQEGKLK----------EVVLKSSKVVRADVCVVGIGAVPATGFLRQS-GIGLDSRGFIPVNKMMQTNVPG 461
Cdd:PRK12770 238 GEGRVEGVELAKMRLGepdesgrprpVPIPGSEFVLEADTVVFAIGEIPTPPFAKEClGIELNRKGEIVVDEKHMTSREG 317
|
330
....*....|.
gi 1900245201 462 VFAAGDAVTFP 472
Cdd:PRK12770 318 VFAAGDVVTGP 328
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
335-467 |
3.38e-12 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 68.64 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 335 VVVVGAGFLGMEVAAYLtekaHSVSV-VEL---EETPFRRFLGErVGRALMKMFENNRVKFYMQTEVSEL-RGQEGKLKe 409
Cdd:PRK06116 170 VAVVGAGYIAVEFAGVL----NGLGSeTHLfvrGDAPLRGFDPD-IRETLVEEMEKKGIRLHTNAVPKAVeKNADGSLT- 243
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 410 VVLKSSKVVRADVCVVGIGAVPAT-GF-LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK06116 244 LTLEDGETLTVDCLIWAIGREPNTdGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGD 303
|
|
| Rieske_RO_Alpha_N |
cd03469 |
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ... |
72-174 |
7.13e-12 |
|
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: 62.61 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFNiSTGDL------ 142
Cdd:cd03469 4 VGHSSELpEPGDYVTLELGGEPLVLVRDrDGEVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYD-LDGKLvgvpre 82
|
90 100 110
....*....|....*....|....*....|....*.
gi 1900245201 143 EDFPGLD----SLHKFQVKIEKEKVYVRASKQALQL 174
Cdd:cd03469 83 EGFPGFDkeklGLRTVPVEEWGGLIFVNLDPDAPPL 118
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
336-501 |
7.34e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 67.92 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 336 VVVGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFLG---ERVGRALMKMFENNRVKFYMQTEVSELRGQEGKlKEVVL 412
Cdd:PRK06370 175 VIIGGGYIGLEFAQMFRRFGSEVTVIERGP----RLLPredEDVAAAVREILEREGIDVRLNAECIRVERDGDG-IAVGL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 413 KS---SKVVRADVCVVGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDavtfplawrnnrkVNIPhWQ 487
Cdd:PRK06370 250 DCnggAPEITGSHILVAVGRVPNTDDlgLEAAGVETDARGYIKVDDQLRTTNPGIYAAGD-------------CNGR-GA 315
|
170
....*....|....*..
gi 1900245201 488 MAH---AQGRVAAQNML 501
Cdd:PRK06370 316 FTHtayNDARIVAANLL 332
|
|
| Rieske_NirD_small_Bacillus |
cd03530 |
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ... |
71-165 |
2.22e-11 |
|
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: 60.31 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 71 AVCHVKDLENGQMREVELGWGKVLLVK-DNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDfPGLD 149
Cdd:cd03530 3 DIGALEDIPPRGARKVQTGGGEIAVFRtADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQG-PDEG 81
|
90
....*....|....*.
gi 1900245201 150 SLHKFQVKIEKEKVYV 165
Cdd:cd03530 82 CVRTFPVKVEDGRVYL 97
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
274-511 |
4.54e-11 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 65.56 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 274 DVRTKKVVFKDGFKLE--YSKLLLAPGSSPKTLSCKG-KE------VENVFTIRTPEdanrvvRLArgrnvvVVGAGFLG 344
Cdd:PRK13748 215 DDQTLIVRLNDGGERVvaFDRCLIATGASPAVPPIPGlKEtpywtsTEALVSDTIPE------RLA------VIGSSVVA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 345 MEVAAYLTEKAHSVSVVELEETPFRRflGERVGRALMKMFENNRVKFYMQTEVSELRGQEGklkEVVLKSSK-VVRADVC 423
Cdd:PRK13748 283 LELAQAFARLGSKVTILARSTLFFRE--DPAIGEAVTAAFRAEGIEVLEHTQASQVAHVDG---EFVLTTGHgELRADKL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 424 VVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPlawrnnrkvniphwQ---MAHAQGRVAAQ 498
Cdd:PRK13748 358 LVATGRAPNTRSLalDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP--------------QfvyVAAAAGTRAAI 423
|
250
....*....|....*
gi 1900245201 499 NMLAQEA--EMSTVP 511
Cdd:PRK13748 424 NMTGGDAalDLTAMP 438
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
284-469 |
4.55e-11 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 65.41 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 284 DGFKLEYSKLLLAPGSSPKTLSCKGKEvenvFTIrtpeDANRVVRLARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVEL 363
Cdd:PTZ00058 197 DGQVIEGKNILIAVGNKPIFPDVKGKE----FTI----SSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 364 EETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGQEGK-LKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIG 442
Cdd:PTZ00058 269 GNRLLRKF-DETIINELENDMKKNNINIITHANVEEIEKVKEKnLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALN 347
|
170 180
....*....|....*....|....*...
gi 1900245201 443 -LDSRGFIPVNKMMQTNVPGVFAAGDAV 469
Cdd:PTZ00058 348 iKTPKGYIKVDDNQRTSVKHIYAVGDCC 375
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
255-467 |
6.76e-11 |
|
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: 64.99 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 255 EFFRAYGieVLTEAQVVTV-DVRTKKVVFKDGFKLEYskLLLAPGSSPKTLSCKGKEV----ENVFTIRTPEdanrvvrl 329
Cdd:TIGR01423 120 TFFLGWG--ALEDKNVVLVrESADPKSAVKERLQAEH--ILLATGSWPQMLGIPGIEHcissNEAFYLDEPP-------- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 330 argRNVVVVGAGFLGMEVAAYLTEKAHSVSVVEL--EETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKL 407
Cdd:TIGR01423 188 ---RRVLTVGGGFISVEFAGIFNAYKPRGGKVTLcyRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGS 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900245201 408 KEVVLKSSKVVRADVCVVGIGAVPATGFLR--QSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:TIGR01423 265 KHVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
318-509 |
1.12e-09 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 60.74 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 318 RTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRF---LGERVGRALMKmfennRVKFYMQ 394
Cdd:PRK07846 154 HTSDTIMRLPELPE--SLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLdddISERFTELASK-----RWDVRLG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 395 TEVSELRGQEGKLkEVVLKSSKVVRADVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVTFP 472
Cdd:PRK07846 227 RNVVGVSQDGSGV-TLRLDDGSTVEADVLLVATGRVPNGDLLdaAAAGVDVDEDGRVVVDEYQRTSAEGVFALGD-VSSP 304
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1900245201 473 lawrnnrkvniphWQMAH---AQGRVAAQNMLAQEAEMST 509
Cdd:PRK07846 305 -------------YQLKHvanHEARVVQHNLLHPDDLIAS 331
|
|
| Rieske_T4moC |
cd03474 |
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ... |
72-166 |
1.99e-09 |
|
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: 55.42 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 72 VCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDfPGLDS 150
Cdd:cd03474 4 VCSLDDVWEGEMELVDVDGEEVLLVaPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGLN-PRDCR 82
|
90
....*....|....*.
gi 1900245201 151 LHKFQVKIEKEKVYVR 166
Cdd:cd03474 83 LARYPVKVEGGDILVD 98
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
409-496 |
2.34e-09 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 59.87 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 409 EVVLKSSKVVRADVCVVGIGAVPAT---GfLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVT--FPLAwrnnrkvni 483
Cdd:PRK07845 252 VVTLTDGRTVEGSHALMAVGSVPNTaglG-LEEAGVELTPSGHITVDRVSRTSVPGIYAAGD-CTgvLPLA--------- 320
|
90
....*....|...
gi 1900245201 484 phwQMAHAQGRVA 496
Cdd:PRK07845 321 ---SVAAMQGRIA 330
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
187-512 |
5.37e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 58.97 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 187 PSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpydrpklsksLDTQPEqlalrPKEFFRaYGI---- 262
Cdd:PRK12814 186 PERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTI-------------------FDANEQ-----AGGMMR-YGIprfr 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 263 --EVLTEAQV-----VTVDVRTKKVVFKD----GFKLEYSKLLLAPGSS-PKTLSCKGKEVENVFT-IRTPEDANRVVRL 329
Cdd:PRK12814 241 lpESVIDADIaplraMGAEFRFNTVFGRDitleELQKEFDAVLLAVGAQkASKMGIPGEELPGVISgIDFLRNVALGTAL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 330 ARGRNVVVVGAGFLGMEVA-AYLTEKAHSVSVV---ELEETPFRRF-----LGERVG-------RALMKMfeNNRVKFym 393
Cdd:PRK12814 321 HPGKKVVVIGGGNTAIDAArTALRLGAESVTILyrrTREEMPANRAeieeaLAEGVSlrelaapVSIERS--EGGLEL-- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 394 qTEVSELRG---QEGKLKEVVLKSSK-VVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNVPGVFAAGDA 468
Cdd:PRK12814 397 -TAIKMQQGepdESGRRRPVPVEGSEfTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPeTLQTSVAGVFAGGDC 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1900245201 469 VTFP-LAWRnnrkvniphwqmAHAQGRVAAQN----MLAQEAEMSTVPY 512
Cdd:PRK12814 476 VTGAdIAIN------------AVEQGKRAAHAidlfLNGKPVTAPVQPF 512
|
|
| PRK09965 |
PRK09965 |
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional |
71-165 |
1.01e-08 |
|
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
Pssm-ID: 170182 [Multi-domain] Cd Length: 106 Bit Score: 53.24 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 71 AVCHVKDLENGQMREVELGwGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLS-RGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:PRK09965 5 YACPVADLPEGEALRVDTS-PVIALFNVGGEFYAIDDRCSHGNASLSEGYLEdDATVECPLHAASFCLRTGKALCLPATD 83
|
90
....*....|....*.
gi 1900245201 150 SLHKFQVKIEKEKVYV 165
Cdd:PRK09965 84 PLRTYPVHVEGGDIFI 99
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
197-472 |
1.37e-08 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 57.48 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCA-----ETLRQEGFSDRI---VLCTLDRH----LPY-DRPKLSKSLdtqpeqlalrpKEFFRAYGIE 263
Cdd:PRK15317 214 VLVVGGGPAGAAAAiyaarKGIRTGIVAERFggqVLDTMGIEnfisVPEtEGPKLAAAL-----------EEHVKEYDVD 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 264 VLTEAQVVTVDVRT--KKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGkEVENVftirtpedaNRVVR--------LARGR 333
Cdd:PRK15317 283 IMNLQRASKLEPAAglIEVELANGAVLKAKTVILATGARWRNMNVPG-EDEYR---------NKGVAycphcdgpLFKGK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 334 NVVVVGAGFLGMEVAAYLTEKAHSVSVVEleetpfrrFLGE-RVGRALM-KMFENNRVKFYMQTEVSELRGQEGKL---- 407
Cdd:PRK15317 353 RVAVIGGGNSGVEAAIDLAGIVKHVTVLE--------FAPElKADQVLQdKLRSLPNVTIITNAQTTEVTGDGDKVtglt 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1900245201 408 -KEVVLKSSKVVRADVCVVGIGAVPATGFLRQSgIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFP 472
Cdd:PRK15317 425 yKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVP 489
|
|
| Reductase_C |
pfam14759 |
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ... |
512-562 |
1.84e-08 |
|
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: 51.80 E-value: 1.84e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1900245201 512 YLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMN 562
Cdd:pfam14759 1 WFWSDQYDLKLQIAGLPTGADEVVLRGDPEDGAFSVFYLRDGRLVAVDAVN 51
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
337-467 |
3.28e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 56.30 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 337 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlgERVGRALMKMF-ENNRVKFYMQTEVSELRGQEGKLkeVVLKSS 415
Cdd:PRK07251 162 IIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE--EPSVAALAKQYmEEDGITFLLNAHTTEVKNDGDQV--LVVTED 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1900245201 416 KVVRADVCVVGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK07251 238 ETYRFDALLYATGRKPNTEplGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| HcaE |
COG4638 |
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ... |
72-156 |
3.89e-08 |
|
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: 54.99 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN-----ISTGDLED 144
Cdd:COG4638 30 VGHSSELpEPGDYLTRTILGEPVVLVRDkDGEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDldgrlVGIPHMEG 109
|
90
....*....|....*.
gi 1900245201 145 FPGLD----SLHKFQV 156
Cdd:COG4638 110 FPDFDparaGLRSVPV 125
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
197-500 |
7.59e-08 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 55.27 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFSdrivlCTLdrhlpYD-RPKLSKsldtqpeqlALRpkeffraYGI-------EVL-TE 267
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHA-----VTI-----FEaGPKLGG---------MMR-------YGIpayrlprEVLdAE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 268 AQVVT---VDVRTKKVVFKD--GFKLE--YSKLLLAPG-SSPKTLSCKGKEVENVFT----IRTPEDANRVvrlARGRNV 335
Cdd:PRK12771 194 IQRILdlgVEVRLGVRVGEDitLEQLEgeFDAVFVAIGaQLGKRLPIPGEDAAGVLDavdfLRAVGEGEPP---FLGKRV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 336 VVVGAGFLGMEVAAylTEK---AHSVSVV-------------ELEE------------TPfRRFLGERVGRALMKMfenn 387
Cdd:PRK12771 271 VVIGGGNTAMDAAR--TARrlgAEEVTIVyrrtredmpahdeEIEEalregveinwlrTP-VEIEGDENGATGLRV---- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 388 rVKFYMQTEVSELRGQEGKLKEVVLKsskvvrADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKM-MQTNVPGVFAAG 466
Cdd:PRK12771 344 -ITVEKMELDEDGRPSPVTGEEETLE------ADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPNfMMTGRPGVFAGG 416
|
330 340 350
....*....|....*....|....*....|....
gi 1900245201 467 DAVTFPlawrnnRKVNiphwqMAHAQGRVAAQNM 500
Cdd:PRK12771 417 DMVPGP------RTVT-----TAIGHGKKAARNI 439
|
|
| PobA |
COG5749 |
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]; |
56-149 |
7.94e-08 |
|
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
Pssm-ID: 444459 [Multi-domain] Cd Length: 349 Bit Score: 54.62 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 56 STPHPYPSPQDCVEA--AVCHVKDLENGQMREVELgWGK-VLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWH 131
Cdd:COG5749 5 RQGPGFNQPFIFRNHwyPVAPSEDLKPNKPKPVTL-LGEpLVIWRDsDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYH 83
|
90
....*....|....*...
gi 1900245201 132 GACFNiSTGDLEDFPGLD 149
Cdd:COG5749 84 GWQFD-GDGKCVHIPQLP 100
|
|
| QcrA/PetC |
COG0723 |
Rieske Fe-S protein [Energy production and conversion]; |
75-165 |
2.26e-07 |
|
Rieske Fe-S protein [Energy production and conversion];
Pssm-ID: 440487 [Multi-domain] Cd Length: 118 Bit Score: 49.61 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 75 VKDLENGQMREVELGWGKVLLVK----DNGEFHALGHKCPHYGAPlVKGVLSRGRVRCPWHGACFNIS----TGdledfP 146
Cdd:COG0723 23 LSDLPPGEGKVVEWRGKPVFVVRtpvrGDGEIVAVSAICTHLGCP-VTWNADEGGFDCPCHGSRFDPDgrvlKG-----P 96
|
90
....*....|....*....
gi 1900245201 147 GLDSLHKFQVKIEKEKVYV 165
Cdd:COG0723 97 APRPLPVPPLEVDDDKLLI 115
|
|
| Rieske_RO_Alpha_VanA_DdmC |
cd03532 |
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ... |
100-136 |
2.92e-07 |
|
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: 49.29 E-value: 2.92e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1900245201 100 GEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN 136
Cdd:cd03532 37 GRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFD 73
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
228-518 |
6.16e-07 |
|
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: 52.16 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 228 DRHLPYDRPKLSKSLDTQPEQL------ALRPKE--FFRAYGievlteaqvVTVDVRTKKVVFKDGFKLEYS--KLLLAP 297
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLnwgyrvALREKKvkYENAYA---------EFVDKHRIKATNKKGKEKIYSaeRFLIAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 298 GSSPKTLSCKG-KEV----ENVFTIrtPEDANRVVrlargrnvvVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFl 372
Cdd:TIGR01438 152 GERPRYPGIPGaKELcitsDDLFSL--PYCPGKTL---------VVGASYVALECAGFLAGIGLDVTVM-VRSILLRGF- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 373 GERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSKVVRA--DVCVVGIGAVPATgflrqSGIGLDSRGF-- 448
Cdd:TIGR01438 219 DQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEeyDTVLLAIGRDACT-----RKLNLENVGVki 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1900245201 449 ------IPVNKMMQTNVPGVFAAGDAVtfplawrNNRKVNIPhwqMAHAQGRVAAQNMLAQEAEMSTVPYLWTAMF 518
Cdd:TIGR01438 294 nkktgkIPADEEEQTNVPYIYAVGDIL-------EDKPELTP---VAIQAGRLLAQRLFKGSTVICDYENVPTTVF 359
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
283-468 |
7.96e-07 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 52.22 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 283 KDGFKLEYSKLLLAPGSSPKTLSckGKEVENvFTIRTPEDANRVVRLARgrNVVVVGAGFLGMEVAAYLTekAHSVSVVE 362
Cdd:PTZ00153 268 KSGKEFKVKNIIIATGSTPNIPD--NIEVDQ-KSVFTSDTAVKLEGLQN--YMGIVGMGIIGLEFMDIYT--ALGSEVVS 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 363 LEETP-FRRFLGERVGRALMKMFENNR-VKFYMQTEVSELRG----------------QEGKLKEVVLKSSKVVRADVCV 424
Cdd:PTZ00153 341 FEYSPqLLPLLDADVAKYFERVFLKSKpVRVHLNTLIEYVRAgkgnqpviighserqtGESDGPKKNMNDIKETYVDSCL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1900245201 425 VGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTN------VPGVFAAGDA 468
Cdd:PTZ00153 421 VATGRKPNT-----NNLGLDKlkiqmkRGFVSVDEHLRVLredqevYDNIFCIGDA 471
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
331-466 |
9.59e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 50.69 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 331 RGRNVVVVGAGFLGMEVAAYLTEKAHSVSVV------ELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQE 404
Cdd:pfam13738 154 AGQKVVVIGGYNSAVDAALELVRKGARVTVLyrgsewEDRDSDPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKEITEVD 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900245201 405 GKLKeVVLKSSKVVRA-DVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNVPGVFAAG 466
Cdd:pfam13738 234 VSYK-VHTEDGRKVTSnDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEeTESTNVPGLFLAG 296
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
187-470 |
1.98e-06 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 50.90 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 187 PSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRI--VLCTLDRHLPYDRPKLSksldtQPEQLALRPKEFFRAYGIEV 264
Cdd:PRK12778 424 PEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVfeALHEIGGVLKYGIPEFR-----LPKKIVDVEIENLKKLGVKF 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 265 LTE---AQVVTVDVrtkkvVFKDGFKleysKLLLAPGSS-PKTLSCKGKEVENVFTirTPEDANRV-----------VRL 329
Cdd:PRK12778 499 ETDvivGKTITIEE-----LEEEGFK----GIFIASGAGlPNFMNIPGENSNGVMS--SNEYLTRVnlmdaaspdsdTPI 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 330 ARGRNVVVVGAGFLGMEVAAylTEK---AHSVSVV---ELEETPFRRflgERVGRAlmkmfENNRVKFYMQTEVSELRGQ 403
Cdd:PRK12778 568 KFGKKVAVVGGGNTAMDSAR--TAKrlgAERVTIVyrrSEEEMPARL---EEVKHA-----KEEGIEFLTLHNPIEYLAD 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 404 E-GKLKEVVLK--------------------SSKVVRADVCVVGIGAVPATGFLRQ-SGIGLDSRGFIPVNKMMQTNVPG 461
Cdd:PRK12778 638 EkGWVKQVVLQkmelgepdasgrrrpvaipgSTFTVDVDLVIVSVGVSPNPLVPSSiPGLELNRKGTIVVDEEMQSSIPG 717
|
....*....
gi 1900245201 462 VFAAGDAVT 470
Cdd:PRK12778 718 IYAGGDIVR 726
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
197-472 |
2.08e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 50.54 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFsDRIVLCTLDRH---LPYDRPKLSksldtQPEQLALRPKEFFRAYGIEVLTEAQVVtv 273
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPggvMRYGIPSYR-----LPDEALDKDIAFIEALGVKIHLNTRVG-- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 274 dvrtKKVVFKDgFKLEYSKLLLAPG-SSPKTLSCKGKEVENVFtirtpeDANRVVRLARG------------RNVVVVGA 340
Cdd:PRK13984 358 ----KDIPLEE-LREKHDAVFLSTGfTLGRSTRIPGTDHPDVI------QALPLLREIRDylrgegpkpkipRSLVVIGG 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 341 GFLGMEVAAYLTE------KAHSVSVVELEET---------PFRRFLGERV----GRALMK-MFENNRVKFYMQTEVSEL 400
Cdd:PRK13984 427 GNVAMDIARSMARlqkmeyGEVNVKVTSLERTfeempadmeEIEEGLEEGVviypGWGPMEvVIENDKVKGVKFKKCVEV 506
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1900245201 401 RGQEGKLKEVVLKSSK-VVRADVCVVGIGAVPATGFLRQSgigLDS-----RGFIPVNKMMQTNVPGVFAAGDAVTFP 472
Cdd:PRK13984 507 FDEEGRFNPKFDESDQiIVEADMVVEAIGQAPDYSYLPEE---LKSklefvRGRILTNEYGQTSIPWLFAGGDIVHGP 581
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
197-470 |
2.50e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 50.40 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFSDRI--VLCTLDRHLPYDRP--KLSKSLDTQPEQlalrpkEFFRAYGIEVLTEAQV-- 270
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIfeALHEPGGVLVYGIPefRLPKETVVKKEI------ENIKKLGVKIETNVVVgk 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 271 -VTVDVRTKKVVFKDGFkleyskllLAPGSS-PKTLSCKGKEVENVFTirtpedAN----RV-----------VRLARGR 333
Cdd:PRK12831 217 tVTIDELLEEEGFDAVF--------IGSGAGlPKFMGIPGENLNGVFS------ANefltRVnlmkaykpeydTPIKVGK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 334 NVVVVGAGFLGMEVAAY---LTEKAHSVSVVELEETPFRRflgERVGRAL-----MKMF---------ENNRVKfYMQTE 396
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTalrLGAEVHIVYRRSEEELPARV---EEVHHAKeegviFDLLtnpveilgdENGWVK-GMKCI 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1900245201 397 VSEL--RGQEGKLKEVVLKSSK-VVRADVCVVGIGAVPATGFLRQS-GIGLDSRGFIPVNK-MMQTNVPGVFAAGDAVT 470
Cdd:PRK12831 359 KMELgePDASGRRRPVEIEGSEfVLEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADEeTGLTSKEGVFAGGDAVT 437
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
192-501 |
7.41e-06 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 48.97 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 192 SSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctLDRH------LPYDRP--KLSKSLdtqpeqLALRpKEFFRAYGIE 263
Cdd:PRK12769 325 KSDKRVAIIGAGPAGLACADVLARNGVAVTV----YDRHpeigglLTFGIPafKLDKSL------LARR-REIFSAMGIE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 264 ---------------VLTEAQVVTVDVRTKKVVfKDGFKLEYsklllAPG--SSPKTLSCKGKEVENVftirtPEDANRV 326
Cdd:PRK12769 394 felncevgkdislesLLEDYDAVFVGVGTYRSM-KAGLPNED-----APGvyDALPFLIANTKQVMGL-----EELPEEP 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 327 VRLARGRNVVVVGAGFLGME-VAAYLTEKAHSV-------------SVVEL----EETPFRRFLGERVGRALMKMFENNR 388
Cdd:PRK12769 463 FINTAGLNVVVLGGGDTAMDcVRTALRHGASNVtcayrrdeanmpgSKKEVknarEEGANFEFNVQPVALELNEQGHVCG 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 389 VKFyMQTEVSELRGQeGKLKEVVLKSSKVVR-ADVCVVGIGAVPAT-GFLRQSGIGLDSRGFI--PVNKMM--QTNVPGV 462
Cdd:PRK12769 543 IRF-LRTRLGEPDAQ-GRRRPVPIPGSEFVMpADAVIMAFGFNPHGmPWLESHGVTVDKWGRIiaDVESQYryQTSNPKI 620
|
330 340 350
....*....|....*....|....*....|....*....
gi 1900245201 463 FAAGDAVtfplawRNNRKVniphwQMAHAQGRVAAQNML 501
Cdd:PRK12769 621 FAGGDAV------RGADLV-----VTAMAEGRHAAQGII 648
|
|
| Rieske_RO_Alpha_OMO_CARDO |
cd03548 |
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ... |
76-144 |
1.57e-05 |
|
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole 1,9a-dioxygenase (CARDO) 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. OMO catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline, the second step in the bacterial degradation of quinoline. OMO consists of a reductase component (OMR) and an oxygenase component (OMO) that together function to shuttle electrons from the reduced pyridine nucleotide to the active site of OMO, where O2 activation and 2-oxoquinoline hydroxylation occurs. CARDO, which contains oxygenase (CARDO-O), ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R) components, catalyzes the dihydroxylation at the C1 and C9a positions of carbazole. The oxygenase component of OMO and CARDO contain only alpha subunits arranged in a trimeric structure.
Pssm-ID: 239617 [Multi-domain] Cd Length: 136 Bit Score: 44.72 E-value: 1.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900245201 76 KDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGV--LSRGRVRCPWHGACFNISTGDLED 144
Cdd:cd03548 22 HELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPecFTKGTITCWYHGWTYRLDDGKLVT 92
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
196-285 |
7.71e-05 |
|
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: 41.42 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 196 NVLIVGAGAAGLVCAETLRQEGfSDRIVLCTLDRHLPYDRPKLSKSLdtqpeqlalrpKEFFRAYGIEVLTEAQV--VTV 273
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLG-SKVTVVERRDRLLPGFDPEIAKIL-----------QEKLEKNGIEFLLNTTVeaIEG 68
|
90
....*....|..
gi 1900245201 274 DVRTKKVVFKDG 285
Cdd:pfam00070 69 NGDGVVVVLTDG 80
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
337-467 |
2.49e-04 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 43.85 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 337 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRfLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSK 416
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQL 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1900245201 417 VVraDVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK08010 242 AV--DALLIASGRQPATASLhpENAGIAVNERGAIVVDKYLHTTADNIWAMGD 292
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
195-361 |
4.06e-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: 42.93 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 195 TNVLIVGAGAAGLVCAETLRQEGFsDRIVL-----------------CTLDRHLPYDRpkLS-KSLDTQPEQLALRP--K 254
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGI-DFVVLekaddvggtwrdnrypgLRLDTPSHLYS--LPfFPNWSDDPDFPTGDeiL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 255 EFFRAY----GIE--VLTEAQVVTVDVRTKK----VVFKDGFKLEYSKLLLAPG--SSPKTLSCKGKEvenVFTIRT--P 320
Cdd:COG2072 84 AYLEAYadkfGLRrpIRFGTEVTSARWDEADgrwtVTTDDGETLTARFVVVATGplSRPKIPDIPGLE---DFAGEQlhS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1900245201 321 EDANRVVRLArGRNVVVVGAGFLGMEVAAYLTEKAHSVSVV 361
Cdd:COG2072 161 ADWRNPVDLA-GKRVLVVGTGASAVQIAPELARVAAHVTVF 200
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
193-219 |
4.64e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 42.56 E-value: 4.64e-04
10 20
....*....|....*....|....*..
gi 1900245201 193 SSTNVLIVGAGAAGLVCAETLRQEGFS 219
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHE 28
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
331-469 |
5.07e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 42.36 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 331 RGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETpfrrFLGERVG-RALMKMFENNRVKFYMQTEVSELRGQEGKLKE 409
Cdd:PRK10262 145 RNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG----FRAEKILiKRLMDKVENGNIILHTNRTLEEVTGDQMGVTG 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900245201 410 VVLKSSK----VVRADVC--VVGIGAVPATGFLrQSGIGLDSrGFIPVNKMM-----QTNVPGVFAAGDAV 469
Cdd:PRK10262 221 VRLRDTQnsdnIESLDVAglFVAIGHSPNTAIF-EGQLELEN-GYIKVQSGIhgnatQTSIPGVFAAGDVM 289
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
199-230 |
5.24e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 38.67 E-value: 5.24e-04
10 20 30
....*....|....*....|....*....|..
gi 1900245201 199 IVGAGAAGLVCAETLRQEGFsdRIVLctLDRH 230
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGF--RVLV--LEKR 28
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
197-222 |
5.38e-04 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 42.60 E-value: 5.38e-04
10 20 30
....*....|....*....|....*....|...
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGF-------SDRI 222
Cdd:COG1231 10 VVIVGAGLAGLAAARELRKAGLdvtvleaRDRV 42
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
336-518 |
1.03e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 42.12 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 336 VVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKeVVLKSS 415
Cdd:PTZ00052 186 LIVGASYIGLETAGFLNELGFDVTVA-VRSIPLRGF-DRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIK-VLFSDG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 416 KVVRADVCVVGIGAVPATGFLRQSGIGL---DSRGFIPVNKMmqTNVPGVFAAGDAVtfplawrnnrkVNIPHWQ-MAHA 491
Cdd:PTZ00052 263 TTELFDTVLYATGRKPDIKGLNLNAIGVhvnKSNKIIAPNDC--TNIPNIFAVGDVV-----------EGRPELTpVAIK 329
|
170 180
....*....|....*....|....*..
gi 1900245201 492 QGRVAAQNMLAQEAEMSTVPYLWTAMF 518
Cdd:PTZ00052 330 AGILLARRLFKQSNEFIDYTFIPTTIF 356
|
|
| Rieske_RO_Alpha_PaO |
cd03480 |
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ... |
97-146 |
1.35e-03 |
|
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO) and ACD1 (accelerated cell death 1). 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. PaO expression increases upon physical wounding of plant leaves and is thought to catalyze a key step in chlorophyll degradation. The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of PaO.
Pssm-ID: 239562 [Multi-domain] Cd Length: 138 Bit Score: 39.23 E-value: 1.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1900245201 97 KDNGEFHALGHKCPHYGAPLVKGVLSR-GRVRCPWHGACFNiSTGDLEDFP 146
Cdd:cd03480 48 RNSQQWRAFDDQCPHRLAPLSEGRIDEeGCLECPYHGWSFD-GSGSCQRIP 97
|
|
| Rieske_RO_Alpha_Cao |
cd04337 |
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ... |
76-136 |
1.58e-03 |
|
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the plastid-envelope inner and thylakoid membranes, that catalyzes the conversion of chlorophyllide a to chlorophyllide b. CAO is found not only in plants but also in chlorophytes and prochlorophytes. This domain represents the 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. Cao is closely related to several other plant RO's including Tic 55, a 55 kDa protein associated with protein transport through the inner chloroplast membrane; Ptc 52, a novel 52 kDa protein isolated from chloroplasts; and LLS1/Pao (Lethal-leaf spot 1/pheophorbide a oxygenase).
Pssm-ID: 239829 [Multi-domain] Cd Length: 129 Bit Score: 39.01 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900245201 76 KDLENGQMREVEL---GWgkVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN 136
Cdd:cd04337 25 KDLKMDTMVPFELfgqPW--VLFRDEDGTPGCIRDECAHRACPLSLGKVIEGRIQCPYHGWEYD 86
|
|
| Rieske_RO_Alpha_PhDO_like |
cd03479 |
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ... |
99-158 |
2.18e-03 |
|
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of PhDO and similar proteins including 3-chlorobenzoate 3,4-dioxygenase (CBDO), phenoxybenzoate dioxygenase (POB-dioxygenase) and 3-nitrobenzoate oxygenase (MnbA). 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. PhDO and CBDO are two-component RO systems, containing oxygenase and reductase components. PhDO catalyzes the dihydroxylation of phthalate to form the 4,5-dihydro-cis-dihydrodiol of phthalate (DHD). CBDO, together with CbaC dehydrogenase, converts the environmental pollutant 3CBA to protocatechuate (PCA) and 5-Cl-PCA, which are then metabolized by the chromosomal PCA meta (extradiol) ring fission pathway. POB-dioxygenase catalyzes the initial catabolic step in the angular dioxygenation of phenoxybenzoate, converting mono- and dichlorinated phenoxybenzoates to protocatechuate and chlorophenols. These phenoxybenzoates are metabolic products formed during the degradation of pyrethroid insecticides.
Pssm-ID: 239561 [Multi-domain] Cd Length: 144 Bit Score: 38.77 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900245201 99 NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiSTGDLEDFPGL--DSLHKFQVKI 158
Cdd:cd03479 54 SGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFD-VDGQCLEMPSEppDSQLKQKVRQ 114
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
333-431 |
3.81e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 40.23 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 333 RNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETpfrrfLGERVGRaLMKMF------------------ENNRVKFYMQ 394
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPE-----LGGRAAQ-LHKTFpgldcpqcilepliaeveANPNITVYTG 214
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1900245201 395 TEVSELRGQEGKLKEVVLKSSK---VVRADVCVVGIGAVP 431
Cdd:COG1148 215 AEVEEVSGYVGNFTVTIKKGPReeiEIEVGAIVLATGFKP 254
|
|
| SfcA |
COG0281 |
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ... |
197-230 |
4.16e-03 |
|
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440050 [Multi-domain] Cd Length: 414 Bit Score: 39.99 E-value: 4.16e-03
10 20 30
....*....|....*....|....*....|....*
gi 1900245201 197 VLIVGAGAAGLVCAETLRQEGFS-DRIVLCtlDRH 230
Cdd:COG0281 194 IVINGAGAAGIAIARLLVAAGLSeENIIMV--DSK 226
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
198-303 |
4.46e-03 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 39.65 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 198 LIVGAGAAGLVCAETLRQEGFsdRIVLctLDR-------------------HLpYDRPKLSKSLDTQPEQL--ALR---P 253
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGA--RVLL--LEKnpkvgrkilisgggrcnftNS-EPLPEFLNYYGGNPHFLksALSrftP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900245201 254 K---EFFRAYGIEVLTE------------AQVVT----------VDVRTK-------------KVVFKDGFKLEYSKLLL 295
Cdd:COG2081 76 EdliAFFEGLGIETKEEssgrvfpdsskaSDILRallaelreagVEIRLRtrvtgiekedggfGVETPDGETVRADAVVL 155
|
170
....*....|
gi 1900245201 296 APG--SSPKT 303
Cdd:COG2081 156 ATGglSYPKL 165
|
|
| 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ |
cd08255 |
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ... |
327-379 |
4.77e-03 |
|
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176217 [Multi-domain] Cd Length: 277 Bit Score: 39.18 E-value: 4.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1900245201 327 VRLAR---GRNVVVVGAGFLGMeVAAYLTEKAHSVSVVELEETPFRRFLGERVGRA 379
Cdd:cd08255 90 VRDAEprlGERVAVVGLGLVGL-LAAQLAKAAGAREVVGVDPDAARRELAEALGPA 144
|
|
| |
