|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
179-547 |
1.98e-102 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 315.93 E-value: 1.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 179 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSKSL--DAQPEQLALRPKEFFRAYGIEMLTEAQVV 256
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLagETDEEDLLLRPADFYEENGIDLRLGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 257 TVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRVL-RLARGRNAVVVGAGFLGMEVAAY 335
Cdd:COG1251 81 AIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRaALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 336 LTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAqEGKLQEVVLKSSKVLRADVCVLGIGAV 415
Cdd:COG1251 161 LRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 416 PATGFLRQSGIGLDsRGfIPVNKMMQTNVPGVFAAGDAVTFPLAWRNNRKVniPHWQMAHAQGRVAAQNMLAQEAEIN-T 494
Cdd:COG1251 240 PNTELARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVL--ELVAPAYEQARVAAANLAGGPAAYEgS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568996297 495 VPYLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKSDEVIAVASMN 547
Cdd:COG1251 316 VPSTKLKVFGVDVASAGDAEGDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVG 368
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
200-515 |
1.04e-83 |
|
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: 264.37 E-value: 1.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 200 QEGFSDRIVLctLDR--HLPYDRAKLSKSL---DAQPEQLALRPKEFFRAYGIEMLTEAQVVTVDVRNKKVVFKDGFKLE 274
Cdd:COG0446 1 RLGPDAEITV--IEKgpHHSYQPCGLPYYVgggIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 275 YSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRV---LRLARGRNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEET 351
Cdd:COG0446 79 YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALreaLKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 352 PFRRFLGErVGRALMKMFENNRVKFYMQTEVSELRAQEGklQEVVLKSSKVLRADVCVLGIGAVPATGFLRQSGIGLDSR 431
Cdd:COG0446 159 LLGVLDPE-MAALLEEELREHGVELRLGETVVAIDGDDK--VAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 432 GFIPVNKMMQTNVPGVFAAGDAVTFPLAwRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEINTVPYLWTAMFGksLRYAG 511
Cdd:COG0446 236 GWIKVDETLQTSDPDVYAAGDCAEVPHP-VTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFD--LCIAS 312
|
....
gi 568996297 512 YGEG 515
Cdd:COG0446 313 TGTG 316
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
180-478 |
1.67e-72 |
|
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: 234.52 E-value: 1.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 180 TNVLIVGAGAAGLVCAETLRQEGFsdRIVLCTLDRHLPYDRAKLSKSLDAQPEQ--LALRPKEFFRAY---------GIE 248
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGG--KVTLIEDEGTCPYGGCVLSKALLGAAEApeIASLWADLYKRKeevvkklnnGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 249 MLTEAQVVTVDVRNKKVVFK-----DGFKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRVLRLARGRNAVVV 323
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKRVVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 324 GAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLqEVVLKSSKVL 403
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGV-EVILKDGTEI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568996297 404 RADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAvtfplawrnnRKVNIPHWQMAHAQG 478
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC----------RVGGPELAQNAVAQG 301
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
179-570 |
1.23e-52 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 185.13 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 179 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSKS--LDAQPEQLALRPKEFFRAYGIEMLTEAQVV 256
Cdd:PRK09754 3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSmlLEDSPQLQQVLPANWWQENNVHLHSGVTIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 257 TVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRvLR--LARGRNAVVVGAGFLGMEVAA 334
Cdd:PRK09754 83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAAR-LRevLQPERSVVIVGAGTIGLELAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 335 YLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVseLRAQEGKLQEVVLKSSKVLRADVCVLGIGA 414
Cdd:PRK09754 162 SATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAI--EHVVDGEKVELTLQSGETLQADVVIYGIGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 415 VPATGFLRQSgiGLDSRGFIPVNKMMQTNVPGVFAAGDAVT--FPLAWRNNRKVniphWQMAHAQGRVAAQNMLAQEAEI 492
Cdd:PRK09754 240 SANDQLAREA--NLDTANGIVIDEACRTCDPAIFAGGDVAItrLDNGALHRCES----WENANNQAQIAAAAMLGLPLPL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568996297 493 NTVPYLWTAMFGKSLRYAGYGEGfDDVIIQGDLEELKFVAFYTKSDEVIAVASMNYDPIVSKVAEVLASGRAIRKREV 570
Cdd:PRK09754 314 LPPPWFWSDQYSDNLQFIGDMRG-DDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLL 390
|
|
| Rieske_AIFL_N |
cd03478 |
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ... |
70-156 |
2.97e-51 |
|
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: 171.27 E-value: 2.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 70 ATVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03478 1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
|
....*..
gi 568996297 150 SLHKFQA 156
Cdd:cd03478 81 SLPCYEV 87
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
180-497 |
1.46e-39 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 148.74 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 180 TNVLIVGAGAAGLVCAETLRQEGFSD-RIVLctLDRH--------LPYDrakLSKSLDaqPEQLALRPKEFFRAYGIEML 250
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDaEVTL--IDPNpyhlfqplLPEV---AAGTLS--PDDIAIPLRELLRRAGVRFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 251 TeAQVVTVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDvENVFTIRTPEDA----NRVLRL------ARGRNA 320
Cdd:COG1252 75 Q-GEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDAlalrERLLAAferaerRRLLTI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 321 VVVGAGFLGMEVAAYLTEKAH-------------SVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRA 387
Cdd:COG1252 153 VVVGGGPTGVELAGELAELLRkllrypgidpdkvRITLVEAGPRILPGL-GEKLSEAAEKELEKRGVEVHTGTRVTEVDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 388 qegklQEVVLKSSKVLRADVCVL--GIGAVPatgFLRQSGIGLDSRGFIPVNKMMQT-NVPGVFAAGDAVTFPLAwrnnr 464
Cdd:COG1252 232 -----DGVTLEDGEEIPADTVIWaaGVKAPP---LLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDP----- 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 568996297 465 kvnIPHW-----QMAHAQGRVAAQNMLAQEAEINTVPY 497
Cdd:COG1252 299 ---DGKPvpktaQAAVQQAKVLAKNIAALLRGKPLKPF 333
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
180-484 |
2.05e-35 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 135.25 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 180 TNVLIVGAGAAGLVCAETLRQEGFSdrIVLctLDRHLPYDRAKLSKSLD--------AQPEQLALRPKEFFRAYGIEMLT 251
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLK--TLV--IEGGEPGGQLATTKEIEnypgfpegISGPELAERLREQAERFGAEILL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 252 EaQVVTVDV--RNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGkdvENVFTIR-----TPEDANrvlrLARGRNAVVVG 324
Cdd:COG0492 77 E-EVTSVDKddGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPG---EEEFEGRgvsycATCDGF----FFRGKDVVVVG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 325 AGFLGMEVAAYLTEKAHSVSVVeleetpFRR--FLGERVgrALMKMFENNRVKFYMQTEVSELRAqEGKLQEVVLKSSK- 401
Cdd:COG0492 149 GGDSALEEALYLTKFASKVTLI------HRRdeLRASKI--LVERLRANPKIEVLWNTEVTEIEG-DGRVEGVTLKNVKt 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 402 ----VLRADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFplawrnnrkvniPHWQMAHA- 476
Cdd:COG0492 220 geekELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY------------KYRQAATAa 287
|
....*....
gi 568996297 477 -QGRVAAQN 484
Cdd:COG0492 288 gEGAIAALS 296
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
180-475 |
2.26e-34 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 135.30 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 180 TNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRH-------LPYdraKLSKSLDAQPEQLALRPKEFFRAYGIEMLTE 252
Cdd:PRK13512 2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDmsfancaLPY---YIGEVVEDRKYALAYTPEKFYDRKQITVKTY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 253 AQVVTVDVRNKKVVFKD-----GFKLEYSKLLLAPGSSPKTLtckGKDVENVFTIRTPEDANRV---LRLARGRNAVVVG 324
Cdd:PRK13512 79 HEVIAINDERQTVTVLNrktneQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIdqfIKANQVDKALVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 325 AGFLGMEVAAYLTEKAHSVSVVElEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEgklqeVVLKSSKVLR 404
Cdd:PRK13512 156 AGYISLEVLENLYERGLHPTLIH-RSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNE-----VTFKSGKVEH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 405 ADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVT-----------FPLAWRNNRKVNIPHWQM 473
Cdd:PRK13512 230 YDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITshyrhvdlpasVPLAWGAHRAASIVAEQI 309
|
..
gi 568996297 474 AH 475
Cdd:PRK13512 310 AG 311
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
182-485 |
6.80e-31 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 125.54 E-value: 6.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFSDRIVL-----------CTLdrhlPYDRAKLSKSldaqPEQLALRPKEFFRAYGIEML 250
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNKELEITVyektdivsfgaCGL----PYFVGGFFDD----PNTMIARTPEEFIKSGIDVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 251 TEAQVVTVDVRNKKVVFKDG-----FKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRV---LRLARGRNAVV 322
Cdd:PRK09564 75 TEHEVVKVDAKNKTITVKNLktgsiFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALkelLKDEEIKNIVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 323 VGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFLGERVGRALMKMFEN----NRVKFYMQTEVSELRAqEGKLQEVVLK 398
Cdd:PRK09564 155 IGAGFIGLEAVEAAKHLGKNVRIIQLED----RILPDSFDKEITDVMEEelreNGVELHLNEFVKSLIG-EDKVEGVVTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 399 SSKVlRADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD-AVTFPLAwrNNRKVNIPHWQMAHAQ 477
Cdd:PRK09564 230 KGEY-EADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcATIYNIV--SNKNVYVPLATTANKL 306
|
....*...
gi 568996297 478 GRVAAQNM 485
Cdd:PRK09564 307 GRMVGENL 314
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
182-497 |
1.09e-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: 122.12 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFsdRIVL---------CTLD------------------RHLP----------YDRAKLS 224
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGL--KVALvekgrlggtCLNVgcipskallhaaevaheaRHAAefgisagapsVDWAALM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 225 KSLDAQPEQLALRPKEFFRAYGIEMLT-EAQVV---TVDVRNKKVvfkdgfkLEYSKLLLAPGSSPKTLTCKGKDVENVF 300
Cdd:COG1249 84 ARKDKVVDRLRGGVEELLKKNGVDVIRgRARFVdphTVEVTGGET-------LTADHIVIATGSRPRVPPIPGLDEVRVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 301 TIRTpedanrVLRLAR-GRNAVVVGAGFLGMEVAAYL----TEkahsVSVVELEETPFRRFlGERVGRALMKMFENNRVK 375
Cdd:COG1249 157 TSDE------ALELEElPKSLVVIGGGYIGLEFAQIFarlgSE----VTLVERGDRLLPGE-DPEISEALEKALEKEGID 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 376 FYMQTEVSELRAQEGKLqEVVLKS---SKVLRADVCVLGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNVPGVFAA 450
Cdd:COG1249 226 ILTGAKVTSVEKTGDGV-TVTLEDgggEEAVEADKVLVATGRRPNTDglGLEAAGVELDERGGIKVDEYLRTSVPGIYAI 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568996297 451 GDAVTFP-LAwrnnrkvnipHwqMAHAQGRVAAQNMLAQEAEI---NTVPY 497
Cdd:COG1249 305 GDVTGGPqLA----------H--VASAEGRVAAENILGKKPRPvdyRAIPS 343
|
|
| NirD |
COG2146 |
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ... |
69-155 |
4.54e-25 |
|
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: 99.53 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 69 EATVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGL 148
Cdd:COG2146 3 EVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLGGPAT 82
|
....*..
gi 568996297 149 DSLHKFQ 155
Cdd:COG2146 83 EPLKTYP 89
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
178-489 |
7.58e-22 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 100.19 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 178 SSTNVLIVGAGAAGLVCAETLRQEGFSDRI---VLCTLDRhLPYDRAKLSKSLDAQ-PEQLALRPKEFFRAYGIEMLTEA 253
Cdd:PRK14989 2 SKVRLAIIGNGMVGHRFIEDLLDKADAANFditVFCEEPR-IAYDRVHLSSYFSHHtAEELSLVREGFYEKHGIKVLVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 254 QVVTVDvRNKKVVFKD-GFKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRVLRLA-RGRNAVVVGAGFLGME 331
Cdd:PRK14989 81 RAITIN-RQEKVIHSSaGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACArRSKRGAVVGGGLLGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 332 VAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELrAQEGKLQEVVLK--SSKVLRADVCV 409
Cdd:PRK14989 160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEI-VQEGVEARKTMRfaDGSELEVDFIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 410 LGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVtfplAWrNNRKVNI--PHWQMAhaqgRVAAQNMLA 487
Cdd:PRK14989 239 FSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECA----SW-NNRVFGLvaPGYKMA----QVAVDHLLG 309
|
..
gi 568996297 488 QE 489
Cdd:PRK14989 310 SE 311
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
182-487 |
2.33e-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: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFSdrivlCTL-DRHlpyDRA-----------KLSKS-LDAQPEQLalrpkeffRAYGIE 248
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHE-----VTVfEAL---DKPggllrygipefRLPKDvLDREIELI--------EALGVE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 249 MLTEAQV-VTVDVrnkkvvfkDGFKLEYSKLLLAPGSS-PKTLTCKGKDVENVFtirtpeDANRVLR-----------LA 315
Cdd:COG0493 188 FRTNVEVgKDITL--------DELLEEFDAVFLATGAGkPRDLGIPGEDLKGVH------SAMDFLTavnlgeapdtiLA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 316 RGRNAVVVGAGFLGMEVA--AyLTEKAHSVSVVEL---EETPFRRflgERVGRALMkmfENNRVKFYMQTE--------- 381
Cdd:COG0493 254 VGKRVVVIGGGNTAMDCArtA-LRLGAESVTIVYRrtrEEMPASK---EEVEEALE---EGVEFLFLVAPVeiigdengr 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 382 VSELRAQEGKLQE----------VVLKSSKVLRADVCVLGIGAVPATGFLR-QSGIGLDSRGFIPVNKM-MQTNVPGVFA 449
Cdd:COG0493 327 VTGLECVRMELGEpdesgrrrpvPIEGSEFTLPADLVILAIGQTPDPSGLEeELGLELDKRGTIVVDEEtYQTSLPGVFA 406
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568996297 450 AGDAVTFP--LAWrnnrkvniphwqmAHAQGRVAAQNMLA 487
Cdd:COG0493 407 GGDAVRGPslVVW-------------AIAEGRKAARAIDR 433
|
|
| Rieske |
pfam00355 |
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ... |
72-154 |
1.69e-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: 86.25 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 72 VCHVKDLENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFNIsTGDLEDFPGLD 149
Cdd:pfam00355 5 VCHSSELPEGEPKVVEVGGEPLVVFRDeDGELYALEDRCPHRGAPLSEGkVNGGGRLECPYHGWRFDG-TGKVVKVPAPR 83
|
....*
gi 568996297 150 SLHKF 154
Cdd:pfam00355 84 PLKSY 88
|
|
| Rieske |
cd03467 |
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ... |
71-155 |
1.40e-19 |
|
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: 83.69 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 71 TVCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03467 3 VVGALSELPPGGGRVVVVGGGPVVVVrREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSGPAPR 82
|
....*.
gi 568996297 150 SLHKFQ 155
Cdd:cd03467 83 PLPKYP 88
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
265-497 |
2.22e-19 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 90.99 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 265 VVFKDGFKLEYS--KLLLAPGSSPKtltcKGKDVEnvFTIRTPEDANRVLRLAR-GRNAVVVGAGFLGMEVAAYLTEKAH 341
Cdd:PRK05249 126 VECPDGEVETLTadKIVIATGSRPY----RPPDVD--FDHPRIYDSDSILSLDHlPRSLIIYGAGVIGCEYASIFAALGV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 342 SVSVVELEETPFRrFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLqEVVLKSSKVLRADvCVL---G-IGAVPA 417
Cdd:PRK05249 200 KVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGV-IVHLKSGKKIKAD-CLLyanGrTGNTDG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 418 TGfLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFP-LAwrnnrkvniphwQMAHAQGRVAAQNMLAQEAE--INT 494
Cdd:PRK05249 277 LN-LENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPsLA------------SASMDQGRIAAQHAVGEATAhlIED 343
|
...
gi 568996297 495 VPY 497
Cdd:PRK05249 344 IPT 346
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
182-454 |
1.10e-16 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 82.90 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFS----DRivlctldrhlpYDRA-----------KLSKSL-DAQPEQLalrpkeffRAY 245
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKvtvfER-----------ADRIggllrygipdfKLEKEViDRRIELM--------EAE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 246 GIEMLTEAQV-VTVDVrnkkvvfkDGFKLEYSKLLLAPGSS-PKTLTCKGKDVENV-----FTIrtpeDANRVLR----- 313
Cdd:PRK12810 207 GIEFRTNVEVgKDITA--------EELLAEYDAVFLGTGAYkPRDLGIPGRDLDGVhfamdFLI----QNTRRVLgdete 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 314 ---LARGRNAVVVGAGFLGME-VAAYLTEKAhsVSVVELEET---PFRRFLGERVGRALMKMfennRVK----------F 376
Cdd:PRK12810 275 pfiSAKGKHVVVIGGGDTGMDcVGTAIRQGA--KSVTQRDIMpmpPSRRNKNNPWPYWPMKL----EVSnaheegvereF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 377 YMQTE--------VSELRAQEGKLQ----EVVLKSSKVLRADVCVLGIGAVPA-TGFLRQSGIGLDSRGFIPVNKM-MQT 442
Cdd:PRK12810 349 NVQTKefegengkVTGVKVVRTELGegdfEPVEGSEFVLPADLVLLAMGFTGPeAGLLAQFGVELDERGRVAAPDNaYQT 428
|
330
....*....|..
gi 568996297 443 NVPGVFAAGDAV 454
Cdd:PRK12810 429 SNPKVFAAGDMR 440
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
242-492 |
3.03e-16 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 81.35 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 242 FRAYGIEMLT-EAQVV---TVDVRNKKV----VFKDgfkleyskLLLAPGSSPKTLtcKGKDVENVfTIRTPEDAnrvLR 313
Cdd:PRK06416 102 LKKNKVDIIRgEAKLVdpnTVRVMTEDGeqtyTAKN--------IILATGSRPREL--PGIEIDGR-VIWTSDEA---LN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 314 LAR-GRNAVVVGAGFLGMEVA-AYLTEKAHsVSVVELEEtpfrRFLG---ERVGRALMKMFENNRVKFYmqTEVSELRAQ 388
Cdd:PRK06416 168 LDEvPKSLVVIGGGYIGVEFAsAYASLGAE-VTIVEALP----RILPgedKEISKLAERALKKRGIKIK--TGAKAKKVE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 389 EGKlQEVVLK-----SSKVLRADVCVLGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTNVPGVFAAGDAVTFP 457
Cdd:PRK06416 241 QTD-DGVTVTledggKEETLEADYVLVAVGRRPNT-----ENLGLEElgvktdRGFIEVDEQLRTNVPNIYAIGDIVGGP 314
|
250 260 270
....*....|....*....|....*....|....*...
gi 568996297 458 lawrnnrkvniphwQMAH---AQGRVAAQNMLAQEAEI 492
Cdd:PRK06416 315 --------------MLAHkasAEGIIAAEAIAGNPHPI 338
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
182-506 |
6.32e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 80.61 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGfsDRIVLctldrhlpYDRAKL-----------SKSLDAQPEQLALRPKefFRAYGIEml 250
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLG--KKVAL--------IEKGPLggtclnvgcipSKALIAAAEAFHEAKH--AEEFGIH-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 251 teAQVVTVD----------VRNKKVVFKDGFKLEYSKLLLAPGS----SPKTLTCKGKDVE--NVFtI----RTP----- 305
Cdd:PRK06292 72 --ADGPKIDfkkvmarvrrERDRFVGGVVEGLEKKPKIDKIKGTarfvDPNTVEVNGERIEakNIV-IatgsRVPpipgv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 306 --EDANR------VLRLAR-GRNAVVVGAGFLGMEVAAYLtekaHS----VSVVELEEtpfrRFLG---ERVGRALMKMF 369
Cdd:PRK06292 149 wlILGDRlltsddAFELDKlPKSLAVIGGGVIGLELGQAL----SRlgvkVTVFERGD----RILPledPEVSKQAQKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 370 ENnRVKFYMQTEVSELRaQEGKLQEVVLKS---SKVLRADVCVLGIGAVPAT---GfLRQSGIGLDSRGFIPVNKMMQTN 443
Cdd:PRK06292 221 SK-EFKIKLGAKVTSVE-KSGDEKVEELEKggkTETIEADYVLVATGRRPNTdglG-LENTGIELDERGRPVVDEHTQTS 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996297 444 VPGVFAAGDAVTFPLawrnnrkvniphwqMAHA---QGRVAAQNMLAQEAE-INTVPYLWT-------AMFGKS 506
Cdd:PRK06292 298 VPGIYAAGDVNGKPP--------------LLHEaadEGRIAAENAAGDVAGgVRYHPIPSVvftdpqiASVGLT 357
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
246-507 |
1.24e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 79.58 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 246 GIEMLTEAQVVTV------------DVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDVENVFtirtpeDANRVLR 313
Cdd:PRK06327 105 GIEGLFKKNKITVlkgrgsfvgktdAGYEIKVTGEDETVITAKHVIIATGSEPRHLPGVPFDNKIIL------DNTGALN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 314 L-ARGRNAVVVGAGFLGMEVAAYLTEKAHSVSVveLEETPfrRFLG---ERVGRALMKMFENNRVKFYMQTEVSELRAQE 389
Cdd:PRK06327 179 FtEVPKKLAVIGAGVIGLELGSVWRRLGAEVTI--LEALP--AFLAaadEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 390 GKLQ---EVVLKSSKVLRADVCVLGIGAVPATGFLRQSGIGL--DSRGFIPVNKMMQTNVPGVFAAGDAVtfplawrnnR 464
Cdd:PRK06327 255 KGVSvayTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLklDERGFIPVDDHCRTNVPNVYAIGDVV---------R 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568996297 465 KvniphWQMAHA---QGRVAAQNMLAQEAEIN--TVPY-LWT----AMFGKSL 507
Cdd:PRK06327 326 G-----PMLAHKaeeEGVAVAERIAGQKGHIDynTIPWvIYTspeiAWVGKTE 373
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
179-452 |
1.92e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 78.42 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 179 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSK--SLDAQPEQLA-LRPKEFFRAYGIEMLTEAQV 255
Cdd:PRK04965 2 SNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHvfSQGQRADDLTrQSAGEFAEQFNLRLFPHTWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 256 VTVDVRNKKVVFKDGfKLEYSKLLLAPGSSPKTLTCKGKdvENVFTIRT-PEDANRVLRLARGRNAVVVGAGFLGMEVAA 334
Cdd:PRK04965 82 TDIDAEAQVVKSQGN-QWQYDKLVLATGASAFVPPIPGR--ELMLTLNSqQEYRAAETQLRDAQRVLVVGGGLIGTELAM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 335 YLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQeVVLKSSKVLRADVCVLGIGA 414
Cdd:PRK04965 159 DLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR-ATLDSGRSIEVDAVIAAAGL 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 568996297 415 VPATGFLRQSGIGLDsRGfIPVNKMMQTNVPGVFAAGD 452
Cdd:PRK04965 238 RPNTALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| Rieske_RO_ferredoxin |
cd03528 |
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ... |
72-140 |
1.97e-15 |
|
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: 72.14 E-value: 1.97e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568996297 72 VCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTG 140
Cdd:cd03528 4 VCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTG 72
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
182-455 |
2.66e-15 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 78.68 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFSdriVlcTL-DRHlpyDRA-----------KLSKSLdaqpeqlALRPKEFFRAYGIEM 249
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYD---V--TIfEAR---DKAggllrygipefRLPKDI-------VDREVERLLKLGVEI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 250 LTEAQV---VTVDvrnkkvvfkDGFKlEYSKLLLAPG-SSPKTLTCKGKDVENVFT----IRTPEDANRVLRLARGRNAV 321
Cdd:PRK11749 208 RTNTEVgrdITLD---------ELRA-GYDAVFIGTGaGLPRFLGIPGENLGGVYSavdfLTRVNQAVADYDLPVGKRVV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 322 VVGAGFLGMEVAAylTEK---AHSVSVV---ELEETP---------------FR------RFLGERVGRALMKmfennrv 374
Cdd:PRK11749 278 VIGGGNTAMDAAR--TAKrlgAESVTIVyrrGREEMPaseeevehakeegveFEwlaapvEILGDEGRVTGVE------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 375 kfYMQTEVSELRAQeGKLQEVVLKSSKVLRADVCVLGIGAVPATGFLR-QSGIGLDSRG-FIPVNKMMQTNVPGVFAAGD 452
Cdd:PRK11749 349 --FVRMELGEPDAS-GRRRVPIEGSEFTLPADLVIKAIGQTPNPLILStTPGLELNRWGtIIADDETGRTSLPGVFAGGD 425
|
...
gi 568996297 453 AVT 455
Cdd:PRK11749 426 IVT 428
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
230-485 |
1.06e-12 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 70.18 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 230 QPeQLALRPKEFFRAYGIEMLTEAQVVTVDVRNKKV-VFKDGFKLEYSKLLLAPGSSPKTLTCKG--------KDVENVF 300
Cdd:PTZ00318 69 RP-ALAKLPNRYLRAVVYDVDFEEKRVKCGVVSKSNnANVNTFSVPYDKLVVAHGARPNTFNIPGveerafflKEVNHAR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 301 TIR---------------TPEDANRVLRLargrnaVVVGAGFLGMEVAAYLTE--------------KAHSVSVVELEET 351
Cdd:PTZ00318 148 GIRkrivqcieraslpttSVEERKRLLHF------VVVGGGPTGVEFAAELADffrddvrnlnpelvEECKVTVLEAGSE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 352 PFRRFlGERVGRALMKMFENNRVKFYMQTEVSELraqegKLQEVVLKSSKVLRADVCV--LGIGAVPATgflRQSGIGLD 429
Cdd:PTZ00318 222 VLGSF-DQALRKYGQRRLRRLGVDIRTKTAVKEV-----LDKEVVLKDGEVIPTGLVVwsTGVGPGPLT---KQLKVDKT 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568996297 430 SRGFIPVNKMMQT-NVPGVFAAGDAVTfplawrNNRKVNIPHWQMAHAQGRVAAQNM 485
Cdd:PTZ00318 293 SRGRISVDDHLRVkPIPNVFALGDCAA------NEERPLPTLAQVASQQGVYLAKEF 343
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
234-453 |
1.47e-12 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 70.23 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 234 LALRPKEFFRAYGI--EMLTEAQVV-------TVDVRNKKVVFKDGFKLEYS--KLLLAPGSSPKTLTCKGKDVEnvfti 302
Cdd:PLN02507 116 LQKKTDEILRLNGIykRLLANAGVKlyegegkIVGPNEVEVTQLDGTKLRYTakHILIATGSRAQRPNIPGKELA----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 303 RTPEDANRVLRLARgrNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERvgRALM-KMFENNRVKFYMQTE 381
Cdd:PLN02507 191 ITSDEALSLEELPK--RAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEM--RAVVaRNLEGRGINLHPRTN 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996297 382 VSELRAQEGKLQeVVLKSSKVLRADVCVLGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDA 453
Cdd:PLN02507 267 LTQLTKTEGGIK-VITDHGEEFVADVVLFATGRAPNTKRlnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
321-452 |
2.77e-12 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 69.03 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 321 VVVGAGFLGMEVAAYLtekaHSVSV-VEL---EETPFRRFLGErVGRALMKMFENNRVKFYMQTEVSELRAQ-EGKLQeV 395
Cdd:PRK06116 171 AVVGAGYIAVEFAGVL----NGLGSeTHLfvrGDAPLRGFDPD-IRETLVEEMEKKGIRLHTNAVPKAVEKNaDGSLT-L 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568996297 396 VLKSSKVLRADVCVLGIGAVPAT-GF-LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 452
Cdd:PRK06116 245 TLEDGETLTVDCLIWAIGREPNTdGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGD 303
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
182-457 |
3.99e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 67.71 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpYDRaklsksldaQPEQLAL--------R-PKEFFRAyGIEMLTE 252
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGYEVHV----------YDK---------LPEPGGLmlfgipefRiPIERVRE-GVKELEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 253 AQVVTVDvrNKKVVF-------------KDGFKLE-----YSKLLLAPGS-SPKTLTCKGKDVENV-------FTIRTPE 306
Cdd:PRK12770 81 AGVVFHT--RTKVCCgeplheeegdefvERIVSLEelvkkYDAVLIATGTwKSRKLGIPGEDLPGVysaleylFRIRAAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 307 ----DANRVLRLArGRNAVVVGAGFLGMEVA--AYLtEKAHSVSVV---ELEETPFRRFLGERVGRALMKMFEN-NRVKF 376
Cdd:PRK12770 159 lgylPWEKVPPVE-GKKVVVVGAGLTAVDAAleAVL-LGAEKVYLAyrrTINEAPAGKYEIERLIARGVEFLELvTPVRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 377 YMQTEVSELRAQEGKLQ----------EVVLKSSKVLRADVCVLGIGAVPATGFLRQS-GIGLDSRGFIPVNKMMQTNVP 445
Cdd:PRK12770 237 IGEGRVEGVELAKMRLGepdesgrprpVPIPGSEFVLEADTVVFAIGEIPTPPFAKEClGIELNRKGEIVVDEKHMTSRE 316
|
330
....*....|..
gi 568996297 446 GVFAAGDAVTFP 457
Cdd:PRK12770 317 GVFAAGDVVTGP 328
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
181-503 |
4.76e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 68.31 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 181 NVLIVGAGAAGLVCAETLRQEGFsdRIVLctLDRHL-----------PydraklSKSL--DAQPEQLALRPKEffraYGI 247
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGM--KVAL--IERGLlggtcvntgcvP------TKTLiaSARAAHLARRAAE----YGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 248 emlTEAQVVTVDVrnKKVV-FKDGFKleysklllapGSSPKTLTCKGKDVENVFTIR---TPEDANRVL---RLARGRNA 320
Cdd:PRK06370 73 ---SVGGPVSVDF--KAVMaRKRRIR----------ARSRHGSEQWLRGLEGVDVFRghaRFESPNTVRvggETLRAKRI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 321 VV-VGA-----GFLGMEVAAYLTekahSVSVVELEETP------------------FRRF--------LGER-------- 360
Cdd:PRK06370 138 FInTGAraaipPIPGLDEVGYLT----NETIFSLDELPehlviigggyiglefaqmFRRFgsevtvieRGPRllpreded 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 361 VGRALMKMFENNRVKFYMQTEVSEL-RAQEGKLQEVVLKS-SKVLRADVCVLGIGAVPATGF--LRQSGIGLDSRGFIPV 436
Cdd:PRK06370 214 VAAAVREILEREGIDVRLNAECIRVeRDGDGIAVGLDCNGgAPEITGSHILVAVGRVPNTDDlgLEAAGVETDARGYIKV 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568996297 437 NKMMQTNVPGVFAAGDavtfplawrnnrkVNIPhWQMAH---AQGRVAAQNML---AQEAEINTVPYlwtAMF 503
Cdd:PRK06370 294 DDQLRTTNPGIYAAGD-------------CNGR-GAFTHtayNDARIVAANLLdggRRKVSDRIVPY---ATY 349
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
319-399 |
1.06e-11 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 60.68 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 319 NAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPfRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKlQEVVLK 398
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL-LPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDG-VVVVLT 78
|
.
gi 568996297 399 S 399
Cdd:pfam00070 79 D 79
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
240-452 |
1.35e-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: 66.92 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 240 EFFRAYGieMLTEAQVVTV-DVRNKKVVFKDGFKLEYskLLLAPGSSPKTLTCKGKD--VENVFTIRTPEDANRVLrlar 316
Cdd:TIGR01423 120 TFFLGWG--ALEDKNVVLVrESADPKSAVKERLQAEH--ILLATGSWPQMLGIPGIEhcISSNEAFYLDEPPRRVL---- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 317 grnavVVGAGFLGMEVAAYLTEKAHSVSVVEL--EETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQE 394
Cdd:TIGR01423 192 -----TVGGGFISVEFAGIFNAYKPRGGKVTLcyRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKH 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 395 VVLKSSKVLRADVCVLGIGAVPATGFLR--QSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 452
Cdd:TIGR01423 267 VTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| Rieske_RO_Alpha_N |
cd03469 |
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ... |
72-154 |
1.61e-11 |
|
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: 61.45 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFNiSTGDLEDFPGL 148
Cdd:cd03469 4 VGHSSELpEPGDYVTLELGGEPLVLVRDrDGEVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYD-LDGKLVGVPRE 82
|
....*.
gi 568996297 149 DSLHKF 154
Cdd:cd03469 83 EGFPGF 88
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
259-502 |
1.68e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 63.63 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 259 DVRNKKVVFKDGFKLE--YSKLLLAPGSSPKTLTCKG-KD------VENVFTIRTPEdanrvlRLArgrnavVVGAGFLG 329
Cdd:PRK13748 215 DDQTLIVRLNDGGERVvaFDRCLIATGASPAVPPIPGlKEtpywtsTEALVSDTIPE------RLA------VIGSSVVA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 330 MEVAAYLTEKAHSVSVVELEETPFRRflGERVGRALMKMFENNRVKFYMQTEVSELRAQEGklqEVVLKSSK-VLRADVC 408
Cdd:PRK13748 283 LELAQAFARLGSKVTILARSTLFFRE--DPAIGEAVTAAFRAEGIEVLEHTQASQVAHVDG---EFVLTTGHgELRADKL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 409 VLGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPlawrnnrkvniphwQ---MAHAQGRVAAQ 483
Cdd:PRK13748 358 LVATGRAPNTRSLalDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP--------------QfvyVAAAAGTRAAI 423
|
250
....*....|....*....
gi 568996297 484 NMLAQEAEINTvpylwTAM 502
Cdd:PRK13748 424 NMTGGDAALDL-----TAM 437
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
269-454 |
2.79e-10 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 63.10 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 269 DGFKLEYSKLLLAPGSSPKTLTCKGKDvenvFTIrtpeDANRVLRLARGRNAVVVGAGFLGMEVAAYLTEKAHSVSVVEL 348
Cdd:PTZ00058 197 DGQVIEGKNILIAVGNKPIFPDVKGKE----FTI----SSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 349 EETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSEL-RAQEGKLQEVVLKSSKVLRADVCVLGIGAVPATGFLRQSGIG 427
Cdd:PTZ00058 269 GNRLLRKF-DETIINELENDMKKNNINIITHANVEEIeKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALN 347
|
170 180
....*....|....*....|....*...
gi 568996297 428 -LDSRGFIPVNKMMQTNVPGVFAAGDAV 454
Cdd:PTZ00058 348 iKTPKGYIKVDDNQRTSVKHIYAVGDCC 375
|
|
| Rieske_NirD_small_Bacillus |
cd03530 |
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ... |
71-140 |
1.41e-09 |
|
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: 55.30 E-value: 1.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996297 71 TVCHVKDLENGQMREVELGWGKVLLVK-DNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTG 140
Cdd:cd03530 3 DIGALEDIPPRGARKVQTGGGEIAVFRtADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETG 73
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
279-481 |
4.13e-09 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 59.10 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 279 LLAPGSSPKTLTCKGKDVENVFTIRT-------PEdanrvlRLargrnaVVVGAGFLGMEVAAYLTEKAHSVSVV----- 346
Cdd:PRK07845 144 LIATGASPRILPTAEPDGERILTWRQlydldelPE------HL------IVVGSGVTGAEFASAYTELGVKVTLVssrdr 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 347 ----------ELEETPFRRflgervgRAlMKMFENNRVKfymqtevSELRAQEGklQEVVLKSSKVLRADVCVLGIGAVP 416
Cdd:PRK07845 212 vlpgedadaaEVLEEVFAR-------RG-MTVLKRSRAE-------SVERTGDG--VVVTLTDGRTVEGSHALMAVGSVP 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 417 AT---GfLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVT--FPLAwrnnrkvniphwQMAHAQGRVA 481
Cdd:PRK07845 275 NTaglG-LEEAGVELTPSGHITVDRVSRTSVPGIYAAGD-CTgvLPLA------------SVAAMQGRIA 330
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
322-452 |
1.10e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 57.45 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 322 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlgERVGRALMKMF-ENNRVKFYMQTEVSELRAQEGKLqeVVLKSS 400
Cdd:PRK07251 162 IIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE--EPSVAALAKQYmEEDGITFLLNAHTTEVKNDGDQV--LVVTED 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568996297 401 KVLRADVCVLGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 452
Cdd:PRK07251 238 ETYRFDALLYATGRKPNTEplGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
172-482 |
2.33e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 57.05 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 172 PSAGHSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpydraklsksLDAQPEqlalrPKEFFRaYGI---- 247
Cdd:PRK12814 186 PERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTI-------------------FDANEQ-----AGGMMR-YGIprfr 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 248 --EMLTEAQV-----VTVDVRNKKVVFKD----GFKLEYSKLLLAPGSS-PKTLTCKGKDVENVFT-IRTPEDANRVLRL 314
Cdd:PRK12814 241 lpESVIDADIaplraMGAEFRFNTVFGRDitleELQKEFDAVLLAVGAQkASKMGIPGEELPGVISgIDFLRNVALGTAL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 315 ARGRNAVVVGAGFLGMEVA-AYLTEKAHSVSVV---ELEETPFRRflgERVGRALMkmfENNRVKFYM----------QT 380
Cdd:PRK12814 321 HPGKKVVVIGGGNTAIDAArTALRLGAESVTILyrrTREEMPANR---AEIEEALA---EGVSLRELAapvsiersegGL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 381 EVSELRAQEGKLQE------VVLKSSK-VLRADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNVPGVFAAGD 452
Cdd:PRK12814 395 ELTAIKMQQGEPDEsgrrrpVPVEGSEfTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPeTLQTSVAGVFAGGD 474
|
330 340 350
....*....|....*....|....*....|.
gi 568996297 453 AVTFP-LAWRnnrkvniphwqmAHAQGRVAA 482
Cdd:PRK12814 475 CVTGAdIAIN------------AVEQGKRAA 493
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
213-503 |
2.38e-08 |
|
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: 56.78 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 213 DRHLPYDRAKLSKSLDAQPEQL------ALRPKE--FFRAYGieMLTEAQVVTVDVRNKKVVFKDGfkleySKLLLAPGS 284
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLnwgyrvALREKKvkYENAYA--EFVDKHRIKATNKKGKEKIYSA-----ERFLIATGE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 285 SPKTLTCKGKD-----VENVFTIrtPEDANRVLrlargrnavVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFlGE 359
Cdd:TIGR01438 154 RPRYPGIPGAKelcitSDDLFSL--PYCPGKTL---------VVGASYVALECAGFLAGIGLDVTVM-VRSILLRGF-DQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 360 RVGRALMKMFENNRVKFYMQTEVSELRAQEGKlqeVVLKSSKVLRA-----DVCVLGIGAVPATgflrqSGIGLDSRGF- 433
Cdd:TIGR01438 221 DCANKVGEHMEEHGVKFKRQFVPIKVEQIEAK---VLVEFTDSTNGieeeyDTVLLAIGRDACT-----RKLNLENVGVk 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568996297 434 -------IPVNKMMQTNVPGVFAAGDAVtfplawrNNRKVNIPhwqMAHAQGRVAAQNMLAQEAEINTVPYLWTAMF 503
Cdd:TIGR01438 293 inkktgkIPADEEEQTNVPYIYAVGDIL-------EDKPELTP---VAIQAGRLLAQRLFKGSTVICDYENVPTTVF 359
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
303-486 |
5.58e-08 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 55.35 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 303 RTPEDanrVLRLAR-GRNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRF---LGERVGRALMKmfennRVKFYM 378
Cdd:PRK07846 154 HTSDT---IMRLPElPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLdddISERFTELASK-----RWDVRL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 379 QTEVSELRAQEGKLqEVVLKSSKVLRADVCVLGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVTF 456
Cdd:PRK07846 226 GRNVVGVSQDGSGV-TLRLDDGSTVEADVLLVATGRVPNGDLLdaAAAGVDVDEDGRVVVDEYQRTSAEGVFALGD-VSS 303
|
170 180 190
....*....|....*....|....*....|...
gi 568996297 457 PlawrnnrkvniphWQMAH---AQGRVAAQNML 486
Cdd:PRK07846 304 P-------------YQLKHvanHEARVVQHNLL 323
|
|
| HcaE |
COG4638 |
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ... |
72-149 |
1.17e-07 |
|
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: 53.84 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN-----ISTGDLED 144
Cdd:COG4638 30 VGHSSELpEPGDYLTRTILGEPVVLVRDkDGEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDldgrlVGIPHMEG 109
|
....*
gi 568996297 145 FPGLD 149
Cdd:COG4638 110 FPDFD 114
|
|
| Reductase_C |
pfam14759 |
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ... |
497-547 |
1.30e-07 |
|
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: 49.10 E-value: 1.30e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568996297 497 YLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKSDEVIAVASMN 547
Cdd:pfam14759 1 WFWSDQYDLKLQIAGLPTGADEVVLRGDPEDGAFSVFYLRDGRLVAVDAVN 51
|
|
| PobA |
COG5749 |
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]; |
72-149 |
2.37e-07 |
|
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
Pssm-ID: 444459 [Multi-domain] Cd Length: 349 Bit Score: 53.08 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 72 VCHVKDLENGQMREVELgWGK-VLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiSTGDLEDFPGLD 149
Cdd:COG5749 23 VAPSEDLKPNKPKPVTL-LGEpLVIWRDsDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYHGWQFD-GDGKCVHIPQLP 100
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
172-485 |
2.38e-07 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 53.73 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 172 PSAGHSSSTNVLIVGAGAAGLVCAETLRQEGFSdrivlCTLdrhlpydraklsksLDAQPeQLA--LRpkeffraYGI-- 247
Cdd:PRK12771 130 PAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHA-----VTI--------------FEAGP-KLGgmMR-------YGIpa 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 248 -----EML-TEAQVVT---VDVRNKKVVFKD--GFKLE--YSKLLLAPG-SSPKTLTCKGKDVENVFT----IRTPEDAN 309
Cdd:PRK12771 183 yrlprEVLdAEIQRILdlgVEVRLGVRVGEDitLEQLEgeFDAVFVAIGaQLGKRLPIPGEDAAGVLDavdfLRAVGEGE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 310 RVLRlarGRNAVVVGAGFLGMEVAAylTEK---AHSVSVV-------------ELEE------------TPfRRFLGERV 361
Cdd:PRK12771 263 PPFL---GKRVVVIGGGNTAMDAAR--TARrlgAEEVTIVyrrtredmpahdeEIEEalregveinwlrTP-VEIEGDEN 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 362 GRALMKMfennrVKFYMQTEVSELRAQEGKLQEVVLKsskvlrADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKM-M 440
Cdd:PRK12771 337 GATGLRV-----ITVEKMELDEDGRPSPVTGEEETLE------ADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPNfM 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568996297 441 QTNVPGVFAAGDAVTFPlawrnnRKVNiphwqMAHAQGRVAAQNM 485
Cdd:PRK12771 406 MTGRPGVFAGGDMVPGP------RTVT-----TAIGHGKKAARNI 439
|
|
| Rieske_RO_Alpha_VanA_DdmC |
cd03532 |
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ... |
100-136 |
2.87e-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: 2.87e-07
10 20 30
....*....|....*....|....*....|....*..
gi 568996297 100 GEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN 136
Cdd:cd03532 37 GRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFD 73
|
|
| Rieske_T4moC |
cd03474 |
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ... |
72-140 |
3.58e-07 |
|
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: 48.87 E-value: 3.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 72 VCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTG 140
Cdd:cd03474 4 VCSLDDVWEGEMELVDVDGEEVLLVaPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTG 73
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
412-457 |
4.97e-07 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 52.47 E-value: 4.97e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568996297 412 IGAVPATGFLRQSgIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFP 457
Cdd:PRK15317 445 IGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVP 489
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
182-457 |
1.83e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 50.92 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFsDRIVLCTLDR------------HLPYDraklskSLDaqpeqlalRPKEFFRAYGIEM 249
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKpggvmrygipsyRLPDE------ALD--------KDIAFIEALGVKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 250 LTEAQVVtvdvrnKKVVFKDgFKLEYSKLLLAPG-SSPKTLTCKGKDVENVFtirtpeDANRVLRLARG----------- 317
Cdd:PRK13984 351 HLNTRVG------KDIPLEE-LREKHDAVFLSTGfTLGRSTRIPGTDHPDVI------QALPLLREIRDylrgegpkpki 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 318 -RNAVVVGAGFLGMEVAAYLTE------KAHSVSVVELEET---------PFRRFLGERV----GRALMK-MFENNRVKF 376
Cdd:PRK13984 418 pRSLVVIGGGNVAMDIARSMARlqkmeyGEVNVKVTSLERTfeempadmeEIEEGLEEGVviypGWGPMEvVIENDKVKG 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 377 YMQTEVSELRAQEGKLQEVVLKSSK-VLRADVCVLGIGAVPATGFLRQSgigLDS-----RGFIPVNKMMQTNVPGVFAA 450
Cdd:PRK13984 498 VKFKKCVEVFDEEGRFNPKFDESDQiIVEADMVVEAIGQAPDYSYLPEE---LKSklefvRGRILTNEYGQTSIPWLFAG 574
|
....*..
gi 568996297 451 GDAVTFP 457
Cdd:PRK13984 575 GDIVHGP 581
|
|
| PRK09965 |
PRK09965 |
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional |
72-151 |
5.14e-06 |
|
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
Pssm-ID: 170182 [Multi-domain] Cd Length: 106 Bit Score: 45.54 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 72 VCHVKDLENGQMREVELGwGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLS-RGRVRCPWHGACFNISTGDLEDFPGLDS 150
Cdd:PRK09965 6 ACPVADLPEGEALRVDTS-PVIALFNVGGEFYAIDDRCSHGNASLSEGYLEdDATVECPLHAASFCLRTGKALCLPATDP 84
|
.
gi 568996297 151 L 151
Cdd:PRK09965 85 L 85
|
|
| QcrA/PetC |
COG0723 |
Rieske Fe-S protein [Energy production and conversion]; |
75-138 |
6.23e-06 |
|
Rieske Fe-S protein [Energy production and conversion];
Pssm-ID: 440487 [Multi-domain] Cd Length: 118 Bit Score: 45.38 E-value: 6.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568996297 75 VKDLENGQMREVELGWGKVLLVK----DNGEFHALGHKCPHYGAPlVKGVLSRGRVRCPWHGACFNIS 138
Cdd:COG0723 23 LSDLPPGEGKVVEWRGKPVFVVRtpvrGDGEIVAVSAICTHLGCP-VTWNADEGGFDCPCHGSRFDPD 89
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
256-453 |
6.63e-06 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 49.14 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 256 VTVDVRNKKVVFKDGFKLEYS-------KLLLAPGSSPKTLTCKGKDVENVFTirtpedANRVLRLARGRNAV-VVGAGF 327
Cdd:PTZ00153 249 VQVIYERGHIVDKNTIKSEKSgkefkvkNIIIATGSTPNIPDNIEVDQKSVFT------SDTAVKLEGLQNYMgIVGMGI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 328 LGMEVAAYLTekAHSVSVVELEETP-FRRFLGERVGRALMKMFENNR-VKFYMQTEVSELRAQEGKlQEVVLKSS----- 400
Cdd:PTZ00153 323 IGLEFMDIYT--ALGSEVVSFEYSPqLLPLLDADVAKYFERVFLKSKpVRVHLNTLIEYVRAGKGN-QPVIIGHSerqtg 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568996297 401 ------------KVLRADVCVLGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTN------VPGVFAAGDA 453
Cdd:PTZ00153 400 esdgpkknmndiKETYVDSCLVATGRKPNT-----NNLGLDKlkiqmkRGFVSVDEHLRVLredqevYDNIFCIGDA 471
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
316-451 |
7.63e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 47.99 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 316 RGRNAVVVGAGFLGMEVAAYLTEKAHSVSVV------ELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQE 389
Cdd:pfam13738 154 AGQKVVVIGGYNSAVDAALELVRKGARVTVLyrgsewEDRDSDPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKEITEVD 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568996297 390 GklqEVVLKSS---KVLRADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNVPGVFAAG 451
Cdd:pfam13738 234 V---SYKVHTEdgrKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEeTESTNVPGLFLAG 296
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
182-455 |
1.25e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 48.09 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFSDRI--VLCTLDRHLPYdraklsksldAQPEqlaLR-PKEFFRAYGIEMLTEAQV--V 256
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIfeALHEPGGVLVY----------GIPE---FRlPKETVVKKEIENIKKLGVkiE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 257 TVDVRNKKVVFKDGFKLE-YSKLLLAPGSS-PKTLTCKGKDVENVFTirtpedANRVLR---------------LARGRN 319
Cdd:PRK12831 210 TNVVVGKTVTIDELLEEEgFDAVFIGSGAGlPKFMGIPGENLNGVFS------ANEFLTrvnlmkaykpeydtpIKVGKK 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 320 AVVVGAGFLGMEVAAY---LTEKAHSVSVVELEETPFRRflgERVGRAL-----MKMF---------ENNRVKfYMQTEV 382
Cdd:PRK12831 284 VAVVGGGNVAMDAARTalrLGAEVHIVYRRSEEELPARV---EEVHHAKeegviFDLLtnpveilgdENGWVK-GMKCIK 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568996297 383 SEL--RAQEGKLQEVVLKSSK-VLRADVCVLGIGAVPATGFLRQS-GIGLDSRGFIPVNK-MMQTNVPGVFAAGDAVT 455
Cdd:PRK12831 360 MELgePDASGRRRPVEIEGSEfVLEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADEeTGLTSKEGVFAGGDAVT 437
|
|
| Rieske_RO_Alpha_OMO_CARDO |
cd03548 |
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ... |
76-144 |
1.54e-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: 1.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996297 76 KDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGV--LSRGRVRCPWHGACFNISTGDLED 144
Cdd:cd03548 22 HELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPecFTKGTITCWYHGWTYRLDDGKLVT 92
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
124-455 |
2.86e-05 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 47.04 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 124 GRVrCPWH----GACFNISTGdlEDFPGLDSLHKFQALQLQRRTKVMAKCISPSAGhsssTNVLIVGAGAAGLVCAETLR 199
Cdd:PRK12778 379 GRV-CPQEkqceSKCIHGKMG--EEAVAIGYLERFVADYERESGNISVPEVAEKNG----KKVAVIGSGPAGLSFAGDLA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 200 QEGFsDRIVLCTLdrHLPYDRAKLSKSLDAQPEQLALRPKEFFRAYGIEMLTE---AQVVTVDVrnkkvVFKDGFKleys 276
Cdd:PRK12778 452 KRGY-DVTVFEAL--HEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDvivGKTITIEE-----LEEEGFK---- 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 277 KLLLAPGSS-PKTLTCKGKDVENVFTirTPEDANRV-----------LRLARGRNAVVVGAGFLGMEVAAylTEK---AH 341
Cdd:PRK12778 520 GIFIASGAGlPNFMNIPGENSNGVMS--SNEYLTRVnlmdaaspdsdTPIKFGKKVAVVGGGNTAMDSAR--TAKrlgAE 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 342 SVSVV---ELEETPFRRflgERVGRALMK----MFENNRVKfYMQTE---VSELRAQEGKLQE---------VVLKSSKV 402
Cdd:PRK12778 596 RVTIVyrrSEEEMPARL---EEVKHAKEEgiefLTLHNPIE-YLADEkgwVKQVVLQKMELGEpdasgrrrpVAIPGSTF 671
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568996297 403 -LRADVCVLGIGAVPATGFLRQ-SGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVT 455
Cdd:PRK12778 672 tVDVDLVIVSVGVSPNPLVPSSiPGLELNRKGTIVVDEEMQSSIPGIYAGGDIVR 726
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
322-452 |
3.66e-05 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 46.55 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 322 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRfLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQevVLKSSK 401
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHENQVQ--VHSEHA 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568996297 402 VLRADVCVLGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 452
Cdd:PRK08010 240 QLAVDALLIASGRQPATASLhpENAGIAVNERGAIVVDKYLHTTADNIWAMGD 292
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
166-486 |
1.71e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 44.74 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 166 MAKCISPSAGHSSSTN--VLIVGAGAAGLVCAETLRQEGFSDRIvlctLDRH----------LPydRAKLSKSLDAqpeq 233
Cdd:PRK12769 312 LAKGWRPDLSQVTKSDkrVAIIGAGPAGLACADVLARNGVAVTV----YDRHpeigglltfgIP--AFKLDKSLLA---- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 234 lalRPKEFFRAYGIEMLTEAQVvtvdvrnKKVVFKDGFKLEYSKLLLAPGS--SPKTltckGKDVENV--------FTIR 303
Cdd:PRK12769 382 ---RRREIFSAMGIEFELNCEV-------GKDISLESLLEDYDAVFVGVGTyrSMKA----GLPNEDApgvydalpFLIA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 304 T-------PEDANRVLRLARGRNAVVVGAGFLGME-VAAYLTEKAHSV-------------SVVEL----EETPFRRFLG 358
Cdd:PRK12769 448 NtkqvmglEELPEEPFINTAGLNVVVLGGGDTAMDcVRTALRHGASNVtcayrrdeanmpgSKKEVknarEEGANFEFNV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 359 ERVGRALMKMFENNRVKFyMQTEVSELRAQeGKLQEVVLKSSK-VLRADVCVLGIGAVPAT-GFLRQSGIGLDSRGFI-- 434
Cdd:PRK12769 528 QPVALELNEQGHVCGIRF-LRTRLGEPDAQ-GRRRPVPIPGSEfVMPADAVIMAFGFNPHGmPWLESHGVTVDKWGRIia 605
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568996297 435 PVNKMM--QTNVPGVFAAGDAVtfplawRNNRKVniphwQMAHAQGRVAAQNML 486
Cdd:PRK12769 606 DVESQYryQTSNPKIFAGGDAV------RGADLV-----VTAMAEGRHAAQGII 648
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
181-270 |
2.06e-04 |
|
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: 40.27 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 181 NVLIVGAGAAGLVCAETLRQEGfSDRIVLCTLDRHLPYDRAKLSKSLdaqpeqlalrpKEFFRAYGIEMLTEAQV--VTV 258
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLG-SKVTVVERRDRLLPGFDPEIAKIL-----------QEKLEKNGIEFLLNTTVeaIEG 68
|
90
....*....|..
gi 568996297 259 DVRNKKVVFKDG 270
Cdd:pfam00070 69 NGDGVVVVLTDG 80
|
|
| Rieske_RO_Alpha_PaO |
cd03480 |
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ... |
56-191 |
4.99e-04 |
|
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: 40.38 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 56 PTPQPYPSPQDCVEA--TVCHVKDLENGQMRevelgwGKVLLVKD--------NGEFHALGHKCPHYGAPLVKGVLSR-G 124
Cdd:cd03480 3 PAGGSDSDKFDWREVwyPVAYVEDLDPSRPT------PFTLLGRDlviwwdrnSQQWRAFDDQCPHRLAPLSEGRIDEeG 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568996297 125 RVRCPWHGACFNiSTGDLEDFPgldslhkfQALQLQRR-TKVMAKCIS-PSAghsSSTNVLIVGAGAAG 191
Cdd:cd03480 77 CLECPYHGWSFD-GSGSCQRIP--------QAAEGGKAhTSPRACVASlPTA---VRQGLLFVWPGEPE 133
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
184-215 |
5.01e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 38.67 E-value: 5.01e-04
10 20 30
....*....|....*....|....*....|..
gi 568996297 184 IVGAGAAGLVCAETLRQEGFsdRIVLctLDRH 215
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGF--RVLV--LEKR 28
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
178-204 |
5.46e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 42.56 E-value: 5.46e-04
10 20
....*....|....*....|....*..
gi 568996297 178 SSTNVLIVGAGAAGLVCAETLRQEGFS 204
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHE 28
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
182-207 |
5.64e-04 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 42.60 E-value: 5.64e-04
10 20 30
....*....|....*....|....*....|...
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGF-------SDRI 207
Cdd:COG1231 10 VVIVGAGLAGLAAARELRKAGLdvtvleaRDRV 42
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
321-503 |
1.09e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 41.73 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 321 VVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQeVVLKSS 400
Cdd:PTZ00052 186 LIVGASYIGLETAGFLNELGFDVTVA-VRSIPLRGF-DRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIK-VLFSDG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 401 KVLRADVCVLGIGAVPATGFLRQSGIGL---DSRGFIPVNKMmqTNVPGVFAAGDAVtfplawrnnrkVNIPHWQ-MAHA 476
Cdd:PTZ00052 263 TTELFDTVLYATGRKPDIKGLNLNAIGVhvnKSNKIIAPNDC--TNIPNIFAVGDVV-----------EGRPELTpVAIK 329
|
170 180
....*....|....*....|....*..
gi 568996297 477 QGRVAAQNMLAQEAEINTVPYLWTAMF 503
Cdd:PTZ00052 330 AGILLARRLFKQSNEFIDYTFIPTTIF 356
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
374-453 |
1.43e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 41.38 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 374 VKF--YMQTEVSElrAQEGKLQ----EVVLKSSKVLRADVCVLGIGAVPATG---FLRQSGIGLDSRGFI----PVNKMM 440
Cdd:COG1148 365 VRFirGRVAEIEE--DEGGKLVvtveDTLLGEPVEIEADLVVLATGMVPSEDneeLAKLLKLPLDQDGFFleahPKLRPV 442
|
90
....*....|...
gi 568996297 441 QTNVPGVFAAGDA 453
Cdd:COG1148 443 ETATDGIFLAGAA 455
|
|
| Rieske_RO_Alpha_Cao |
cd04337 |
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ... |
76-136 |
1.56e-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: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996297 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, ... |
99-147 |
3.35e-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: 38.38 E-value: 3.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568996297 99 NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiSTGDLEDFPG 147
Cdd:cd03479 54 SGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFD-VDGQCLEMPS 101
|
|
| SfcA |
COG0281 |
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ... |
182-215 |
4.11e-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: 4.11e-03
10 20 30
....*....|....*....|....*....|....*
gi 568996297 182 VLIVGAGAAGLVCAETLRQEGFS-DRIVLCtlDRH 215
Cdd:COG0281 194 IVINGAGAAGIAIARLLVAAGLSeENIIMV--DSK 226
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
183-204 |
5.52e-03 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 39.26 E-value: 5.52e-03
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
180-451 |
9.88e-03 |
|
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: 38.69 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 180 TNVLIVGAGAAGLVCAETLRQEGFSDRIvlctLD---------RHLPYDRAKL----------SKSLDAQPEQLALRP-- 238
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVV----LEkaddvggtwRDNRYPGLRLdtpshlyslpFFPNWSDDPDFPTGDei 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 239 KEFFRAY----GIE--MLTEAQVVTVDVRNKK----VVFKDGFKLEYSKLLLAPG--SSPKTLTCKGKDvenVFTIRT-- 304
Cdd:COG2072 83 LAYLEAYadkfGLRrpIRFGTEVTSARWDEADgrwtVTTDDGETLTARFVVVATGplSRPKIPDIPGLE---DFAGEQlh 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 305 PEDANRVLRLArGRNAVVVGAGFLGMEVAAYLTEKAHSVSVV--------------------------ELEETPFRRFLG 358
Cdd:COG2072 160 SADWRNPVDLA-GKRVLVVGTGASAVQIAPELARVAAHVTVFqrtppwvlprpnydpergrpanylglEAPPALNRRDAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996297 359 ERVGRALMKMFENNRVKFYMQTEV---------SELR--AQEGKLQ------------EVVLKSSKVLRADVCVLGIGAV 415
Cdd:COG2072 239 AWLRRLLRAQVKDPELGLLTPDYPpgckrpllsTDYYeaLRRGNVElvtggieritedGVVFADGTEHEVDVIVWATGFR 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 568996297 416 PATGFLRQSGI-GLDSRGFIPVNK-MMQTNVPGVFAAG 451
Cdd:COG2072 319 ADLPWLAPLDVrGRDGRSGPRAYLgVVVPGFPNLFFLG 356
|
|
| |
