|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
194-562 |
2.16e-102 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 316.31 E-value: 2.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSKSL--DAQPEQLALRPKEFFRAYGIEMLTEAQVV 271
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLagETDEEDLLLRPADFYEENGIDLRLGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 272 TVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRVL-RLARGRNAVVVGAGFLGMEVAAY 350
Cdd:COG1251 81 AIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRaALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 351 LTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAqEGKLQEVVLKSSKVLRADVCVLGIGAV 430
Cdd:COG1251 161 LRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 431 PATGFLRQSGIGLDsRGfIPVNKMMQTNVPGVFAAGDAVTFPLAWRNNRKVniPHWQMAHAQGRVAAQNMLAQEAEIN-T 509
Cdd:COG1251 240 PNTELARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVL--ELVAPAYEQARVAAANLAGGPAAYEgS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568996291 510 VPYLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKSDEVIAVASMN 562
Cdd:COG1251 316 VPSTKLKVFGVDVASAGDAEGDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVG 368
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
215-530 |
1.61e-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: 1.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 215 QEGFSDRIVLctLDR--HLPYDRAKLSKSL---DAQPEQLALRPKEFFRAYGIEMLTEAQVVTVDVRNKKVVFKDGFKLE 289
Cdd:COG0446 1 RLGPDAEITV--IEKgpHHSYQPCGLPYYVgggIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 290 YSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRV---LRLARGRNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEET 366
Cdd:COG0446 79 YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALreaLKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 367 PFRRFLGErVGRALMKMFENNRVKFYMQTEVSELRAQEGklQEVVLKSSKVLRADVCVLGIGAVPATGFLRQSGIGLDSR 446
Cdd:COG0446 159 LLGVLDPE-MAALLEEELREHGVELRLGETVVAIDGDDK--VAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 447 GFIPVNKMMQTNVPGVFAAGDAVTFPLAwRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEINTVPYLWTAMFGksLRYAG 526
Cdd:COG0446 236 GWIKVDETLQTSDPDVYAAGDCAEVPHP-VTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFD--LCIAS 312
|
....
gi 568996291 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 |
4.23e-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: 234.13 E-value: 4.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 195 TNVLIVGAGAAGLVCAETLRQEGFsdRIVLCTLDRHLPYDRAKLSKSLDAQPEQ--LALRPKEFFRAY---------GIE 263
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGG--KVTLIEDEGTCPYGGCVLSKALLGAAEApeIASLWADLYKRKeevvkklnnGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 264 MLTEAQVVTVDVRNKKVVFK-----DGFKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRVLRLARGRNAVVV 338
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKRVVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 339 GAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLqEVVLKSSKVL 418
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGV-EVILKDGTEI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568996291 419 RADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAvtfplawrnnRKVNIPHWQMAHAQG 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 ... |
70-163 |
1.28e-54 |
|
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: 180.51 E-value: 1.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 70 ATVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03478 1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
|
90
....*....|....
gi 568996291 150 SLHKFQVKIEKEKV 163
Cdd:cd03478 81 SLPCYEVEVEDGRV 94
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
194-585 |
1.59e-52 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 185.13 E-value: 1.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSKS--LDAQPEQLALRPKEFFRAYGIEMLTEAQVV 271
Cdd:PRK09754 3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSmlLEDSPQLQQVLPANWWQENNVHLHSGVTIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 272 TVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRvLR--LARGRNAVVVGAGFLGMEVAA 349
Cdd:PRK09754 83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAAR-LRevLQPERSVVIVGAGTIGLELAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 350 YLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVseLRAQEGKLQEVVLKSSKVLRADVCVLGIGA 429
Cdd:PRK09754 162 SATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAI--EHVVDGEKVELTLQSGETLQADVVIYGIGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 430 VPATGFLRQSgiGLDSRGFIPVNKMMQTNVPGVFAAGDAVT--FPLAWRNNRKVniphWQMAHAQGRVAAQNMLAQEAEI 507
Cdd:PRK09754 240 SANDQLAREA--NLDTANGIVIDEACRTCDPAIFAGGDVAItrLDNGALHRCES----WENANNQAQIAAAAMLGLPLPL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568996291 508 NTVPYLWTAMFGKSLRYAGYGEGfDDVIIQGDLEELKFVAFYTKSDEVIAVASMNYDPIVSKVAEVLASGRAIRKREV 585
Cdd:PRK09754 314 LPPPWFWSDQYSDNLQFIGDMRG-DDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLL 390
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
195-512 |
1.50e-39 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 149.13 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 195 TNVLIVGAGAAGLVCAETLRQEGFSD-RIVLctLDRH--------LPYDrakLSKSLDaqPEQLALRPKEFFRAYGIEML 265
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDaEVTL--IDPNpyhlfqplLPEV---AAGTLS--PDDIAIPLRELLRRAGVRFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 266 TeAQVVTVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDvENVFTIRTPEDA----NRVLRL------ARGRNA 335
Cdd:COG1252 75 Q-GEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDAlalrERLLAAferaerRRLLTI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 336 VVVGAGFLGMEVAAYLTEKAH-------------SVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRA 402
Cdd:COG1252 153 VVVGGGPTGVELAGELAELLRkllrypgidpdkvRITLVEAGPRILPGL-GEKLSEAAEKELEKRGVEVHTGTRVTEVDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 403 qegklQEVVLKSSKVLRADVCVL--GIGAVPatgFLRQSGIGLDSRGFIPVNKMMQT-NVPGVFAAGDAVTFPLAwrnnr 479
Cdd:COG1252 232 -----DGVTLEDGEEIPADTVIWaaGVKAPP---LLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDP----- 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 568996291 480 kvnIPHW-----QMAHAQGRVAAQNMLAQEAEINTVPY 512
Cdd:COG1252 299 ---DGKPvpktaQAAVQQAKVLAKNIAALLRGKPLKPF 333
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
195-499 |
2.33e-35 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 135.25 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 195 TNVLIVGAGAAGLVCAETLRQEGFSdrIVLctLDRHLPYDRAKLSKSLD--------AQPEQLALRPKEFFRAYGIEMLT 266
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLK--TLV--IEGGEPGGQLATTKEIEnypgfpegISGPELAERLREQAERFGAEILL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 267 EaQVVTVDV--RNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGkdvENVFTIR-----TPEDANrvlrLARGRNAVVVG 339
Cdd:COG0492 77 E-EVTSVDKddGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPG---EEEFEGRgvsycATCDGF----FFRGKDVVVVG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 340 AGFLGMEVAAYLTEKAHSVSVVeleetpFRR--FLGERVgrALMKMFENNRVKFYMQTEVSELRAqEGKLQEVVLKSSK- 416
Cdd:COG0492 149 GGDSALEEALYLTKFASKVTLI------HRRdeLRASKI--LVERLRANPKIEVLWNTEVTEIEG-DGRVEGVTLKNVKt 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 417 ----VLRADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFplawrnnrkvniPHWQMAHA- 491
Cdd:COG0492 220 geekELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY------------KYRQAATAa 287
|
....*....
gi 568996291 492 -QGRVAAQN 499
Cdd:COG0492 288 gEGAIAALS 296
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
195-490 |
2.58e-34 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 135.30 E-value: 2.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 195 TNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRH-------LPYdraKLSKSLDAQPEQLALRPKEFFRAYGIEMLTE 267
Cdd:PRK13512 2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDmsfancaLPY---YIGEVVEDRKYALAYTPEKFYDRKQITVKTY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 268 AQVVTVDVRNKKVVFKD-----GFKLEYSKLLLAPGSSPKTLtckGKDVENVFTIRTPEDANRV---LRLARGRNAVVVG 339
Cdd:PRK13512 79 HEVIAINDERQTVTVLNrktneQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIdqfIKANQVDKALVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 340 AGFLGMEVAAYLTEKAHSVSVVElEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEgklqeVVLKSSKVLR 419
Cdd:PRK13512 156 AGYISLEVLENLYERGLHPTLIH-RSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNE-----VTFKSGKVEH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 420 ADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVT-----------FPLAWRNNRKVNIPHWQM 488
Cdd:PRK13512 230 YDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITshyrhvdlpasVPLAWGAHRAASIVAEQI 309
|
..
gi 568996291 489 AH 490
Cdd:PRK13512 310 AG 311
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
197-500 |
7.55e-31 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 125.54 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFSDRIVL-----------CTLdrhlPYDRAKLSKSldaqPEQLALRPKEFFRAYGIEML 265
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNKELEITVyektdivsfgaCGL----PYFVGGFFDD----PNTMIARTPEEFIKSGIDVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 266 TEAQVVTVDVRNKKVVFKDG-----FKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRV---LRLARGRNAVV 337
Cdd:PRK09564 75 TEHEVVKVDAKNKTITVKNLktgsiFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALkelLKDEEIKNIVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 338 VGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFLGERVGRALMKMFEN----NRVKFYMQTEVSELRAqEGKLQEVVLK 413
Cdd:PRK09564 155 IGAGFIGLEAVEAAKHLGKNVRIIQLED----RILPDSFDKEITDVMEEelreNGVELHLNEFVKSLIG-EDKVEGVVTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 414 SSKVlRADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD-AVTFPLAwrNNRKVNIPHWQMAHAQ 492
Cdd:PRK09564 230 KGEY-EADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcATIYNIV--SNKNVYVPLATTANKL 306
|
....*...
gi 568996291 493 GRVAAQNM 500
Cdd:PRK09564 307 GRMVGENL 314
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
197-512 |
1.41e-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: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFsdRIVL---------CTLD------------------RHLP----------YDRAKLS 239
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGL--KVALvekgrlggtCLNVgcipskallhaaevaheaRHAAefgisagapsVDWAALM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 240 KSLDAQPEQLALRPKEFFRAYGIEMLT-EAQVV---TVDVRNKKVvfkdgfkLEYSKLLLAPGSSPKTLTCKGKDVENVF 315
Cdd:COG1249 84 ARKDKVVDRLRGGVEELLKKNGVDVIRgRARFVdphTVEVTGGET-------LTADHIVIATGSRPRVPPIPGLDEVRVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 316 TIRTpedanrVLRLAR-GRNAVVVGAGFLGMEVAAYL----TEkahsVSVVELEETPFRRFlGERVGRALMKMFENNRVK 390
Cdd:COG1249 157 TSDE------ALELEElPKSLVVIGGGYIGLEFAQIFarlgSE----VTLVERGDRLLPGE-DPEISEALEKALEKEGID 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 391 FYMQTEVSELRAQEGKLqEVVLKS---SKVLRADVCVLGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNVPGVFAA 465
Cdd:COG1249 226 ILTGAKVTSVEKTGDGV-TVTLEDgggEEAVEADKVLVATGRRPNTDglGLEAAGVELDERGGIKVDEYLRTSVPGIYAI 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568996291 466 GDAVTFP-LAwrnnrkvnipHwqMAHAQGRVAAQNMLAQEAEI---NTVPY 512
Cdd:COG1249 305 GDVTGGPqLA----------H--VASAEGRVAAENILGKKPRPvdyRAIPS 343
|
|
| NirD |
COG2146 |
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ... |
69-166 |
1.96e-28 |
|
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: 109.16 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 69 EATVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGL 148
Cdd:COG2146 3 EVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLGGPAT 82
|
90
....*....|....*...
gi 568996291 149 DSLHKFQVKIEKEKVTIR 166
Cdd:COG2146 83 EPLKTYPVRVEDGDVYVD 100
|
|
| Rieske |
cd03467 |
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ... |
71-163 |
4.35e-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: 91.01 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 71 TVCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLD 149
Cdd:cd03467 3 VVGALSELPPGGGRVVVVGGGPVVVVrREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSGPAPR 82
|
90
....*....|....
gi 568996291 150 SLHKFQVKIEKEKV 163
Cdd:cd03467 83 PLPKYPVKVEGDGV 96
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
193-504 |
9.79e-22 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 100.19 E-value: 9.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 193 SSTNVLIVGAGAAGLVCAETLRQEGFSDRI---VLCTLDRhLPYDRAKLSKSLDAQ-PEQLALRPKEFFRAYGIEMLTEA 268
Cdd:PRK14989 2 SKVRLAIIGNGMVGHRFIEDLLDKADAANFditVFCEEPR-IAYDRVHLSSYFSHHtAEELSLVREGFYEKHGIKVLVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 269 QVVTVDvRNKKVVFKD-GFKLEYSKLLLAPGSSPKTLTCKGKDVENVFTIRTPEDANRVLRLA-RGRNAVVVGAGFLGME 346
Cdd:PRK14989 81 RAITIN-RQEKVIHSSaGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACArRSKRGAVVGGGLLGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 347 VAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELrAQEGKLQEVVLK--SSKVLRADVCV 424
Cdd:PRK14989 160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEI-VQEGVEARKTMRfaDGSELEVDFIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 425 LGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVtfplAWrNNRKVNI--PHWQMAhaqgRVAAQNMLA 502
Cdd:PRK14989 239 FSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECA----SW-NNRVFGLvaPGYKMA----QVAVDHLLG 309
|
..
gi 568996291 503 QE 504
Cdd:PRK14989 310 SE 311
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
197-502 |
2.58e-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: 96.74 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFSdrivlCTL-DRHlpyDRA-----------KLSKS-LDAQPEQLalrpkeffRAYGIE 263
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHE-----VTVfEAL---DKPggllrygipefRLPKDvLDREIELI--------EALGVE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 264 MLTEAQV-VTVDVrnkkvvfkDGFKLEYSKLLLAPGSS-PKTLTCKGKDVENVFtirtpeDANRVLR-----------LA 330
Cdd:COG0493 188 FRTNVEVgKDITL--------DELLEEFDAVFLATGAGkPRDLGIPGEDLKGVH------SAMDFLTavnlgeapdtiLA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 331 RGRNAVVVGAGFLGMEVA--AyLTEKAHSVSVVEL---EETPFRRflgERVGRALMkmfENNRVKFYMQTE--------- 396
Cdd:COG0493 254 VGKRVVVIGGGNTAMDCArtA-LRLGAESVTIVYRrtrEEMPASK---EEVEEALE---EGVEFLFLVAPVeiigdengr 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 397 VSELRAQEGKLQE----------VVLKSSKVLRADVCVLGIGAVPATGFLR-QSGIGLDSRGFIPVNKM-MQTNVPGVFA 464
Cdd:COG0493 327 VTGLECVRMELGEpdesgrrrpvPIEGSEFTLPADLVILAIGQTPDPSGLEeELGLELDKRGTIVVDEEtYQTSLPGVFA 406
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568996291 465 AGDAVTFP--LAWrnnrkvniphwqmAHAQGRVAAQNMLA 502
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 |
1.31e-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: 86.63 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 72 VCHVKDLENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFNIsTGDLEDFPGLD 149
Cdd:pfam00355 5 VCHSSELPEGEPKVVEVGGEPLVVFRDeDGELYALEDRCPHRGAPLSEGkVNGGGRLECPYHGWRFDG-TGKVVKVPAPR 83
|
....*
gi 568996291 150 SLHKF 154
Cdd:pfam00355 84 PLKSY 88
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
280-512 |
2.34e-19 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 90.99 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 280 VVFKDGFKLEYS--KLLLAPGSSPKtltcKGKDVEnvFTIRTPEDANRVLRLAR-GRNAVVVGAGFLGMEVAAYLTEKAH 356
Cdd:PRK05249 126 VECPDGEVETLTadKIVIATGSRPY----RPPDVD--FDHPRIYDSDSILSLDHlPRSLIIYGAGVIGCEYASIFAALGV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 357 SVSVVELEETPFRrFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLqEVVLKSSKVLRADvCVL---G-IGAVPA 432
Cdd:PRK05249 200 KVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGV-IVHLKSGKKIKAD-CLLyanGrTGNTDG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 433 TGfLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFP-LAwrnnrkvniphwQMAHAQGRVAAQNMLAQEAE--INT 509
Cdd:PRK05249 277 LN-LENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPsLA------------SASMDQGRIAAQHAVGEATAhlIED 343
|
...
gi 568996291 510 VPY 512
Cdd:PRK05249 344 IPT 346
|
|
| Rieske_RO_ferredoxin |
cd03528 |
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ... |
72-166 |
3.66e-18 |
|
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: 79.84 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 72 VCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLDSL 151
Cdd:cd03528 4 VCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPATEPL 83
|
90
....*....|....*
gi 568996291 152 HKFQVKIEKEKVTIR 166
Cdd:cd03528 84 KTYPVKVEDGDVYVD 98
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
197-469 |
1.15e-16 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 82.90 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFS----DRivlctldrhlpYDRA-----------KLSKSL-DAQPEQLalrpkeffRAY 260
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKvtvfER-----------ADRIggllrygipdfKLEKEViDRRIELM--------EAE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 261 GIEMLTEAQV-VTVDVrnkkvvfkDGFKLEYSKLLLAPGSS-PKTLTCKGKDVENV-----FTIrtpeDANRVLR----- 328
Cdd:PRK12810 207 GIEFRTNVEVgKDITA--------EELLAEYDAVFLGTGAYkPRDLGIPGRDLDGVhfamdFLI----QNTRRVLgdete 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 329 ---LARGRNAVVVGAGFLGME-VAAYLTEKAhsVSVVELEET---PFRRFLGERVGRALMKMfennRVK----------F 391
Cdd:PRK12810 275 pfiSAKGKHVVVIGGGDTGMDcVGTAIRQGA--KSVTQRDIMpmpPSRRNKNNPWPYWPMKL----EVSnaheegvereF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 392 YMQTE--------VSELRAQEGKLQ----EVVLKSSKVLRADVCVLGIGAVPA-TGFLRQSGIGLDSRGFIPVNKM-MQT 457
Cdd:PRK12810 349 NVQTKefegengkVTGVKVVRTELGegdfEPVEGSEFVLPADLVLLAMGFTGPeAGLLAQFGVELDERGRVAAPDNaYQT 428
|
330
....*....|..
gi 568996291 458 NVPGVFAAGDAV 469
Cdd:PRK12810 429 SNPKVFAAGDMR 440
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
257-507 |
4.35e-16 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 80.96 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 257 FRAYGIEMLT-EAQVV---TVDVRNKKV----VFKDgfkleyskLLLAPGSSPKTLtcKGKDVENVfTIRTPEDAnrvLR 328
Cdd:PRK06416 102 LKKNKVDIIRgEAKLVdpnTVRVMTEDGeqtyTAKN--------IILATGSRPREL--PGIEIDGR-VIWTSDEA---LN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 329 LAR-GRNAVVVGAGFLGMEVA-AYLTEKAHsVSVVELEEtpfrRFLG---ERVGRALMKMFENNRVKFYmqTEVSELRAQ 403
Cdd:PRK06416 168 LDEvPKSLVVIGGGYIGVEFAsAYASLGAE-VTIVEALP----RILPgedKEISKLAERALKKRGIKIK--TGAKAKKVE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 404 EGKlQEVVLK-----SSKVLRADVCVLGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTNVPGVFAAGDAVTFP 472
Cdd:PRK06416 241 QTD-DGVTVTledggKEETLEADYVLVAVGRRPNT-----ENLGLEElgvktdRGFIEVDEQLRTNVPNIYAIGDIVGGP 314
|
250 260 270
....*....|....*....|....*....|....*...
gi 568996291 473 lawrnnrkvniphwQMAH---AQGRVAAQNMLAQEAEI 507
Cdd:PRK06416 315 --------------MLAHkasAEGIIAAEAIAGNPHPI 338
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
197-521 |
8.59e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 80.22 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGfsDRIVLctldrhlpYDRAKL-----------SKSLDAQPEQLALRPKefFRAYGIEml 265
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLG--KKVAL--------IEKGPLggtclnvgcipSKALIAAAEAFHEAKH--AEEFGIH-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 266 teAQVVTVD----------VRNKKVVFKDGFKLEYSKLLLAPGS----SPKTLTCKGKDVE--NVFtI----RTP----- 320
Cdd:PRK06292 72 --ADGPKIDfkkvmarvrrERDRFVGGVVEGLEKKPKIDKIKGTarfvDPNTVEVNGERIEakNIV-IatgsRVPpipgv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 321 --EDANR------VLRLAR-GRNAVVVGAGFLGMEVAAYLtekaHS----VSVVELEEtpfrRFLG---ERVGRALMKMF 384
Cdd:PRK06292 149 wlILGDRlltsddAFELDKlPKSLAVIGGGVIGLELGQAL----SRlgvkVTVFERGD----RILPledPEVSKQAQKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 385 ENnRVKFYMQTEVSELRaQEGKLQEVVLKS---SKVLRADVCVLGIGAVPAT---GfLRQSGIGLDSRGFIPVNKMMQTN 458
Cdd:PRK06292 221 SK-EFKIKLGAKVTSVE-KSGDEKVEELEKggkTETIEADYVLVATGRRPNTdglG-LENTGIELDERGRPVVDEHTQTS 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996291 459 VPGVFAAGDAVTFPLawrnnrkvniphwqMAHA---QGRVAAQNMLAQEAE-INTVPYLWT-------AMFGKS 521
Cdd:PRK06292 298 VPGIYAAGDVNGKPP--------------LLHEaadEGRIAAENAAGDVAGgVRYHPIPSVvftdpqiASVGLT 357
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
261-522 |
1.83e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 79.20 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 261 GIEMLTEAQVVTV------------DVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDVENVFtirtpeDANRVLR 328
Cdd:PRK06327 105 GIEGLFKKNKITVlkgrgsfvgktdAGYEIKVTGEDETVITAKHVIIATGSEPRHLPGVPFDNKIIL------DNTGALN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 329 L-ARGRNAVVVGAGFLGMEVAAYLTEKAHSVSVveLEETPfrRFLG---ERVGRALMKMFENNRVKFYMQTEVSELRAQE 404
Cdd:PRK06327 179 FtEVPKKLAVIGAGVIGLELGSVWRRLGAEVTI--LEALP--AFLAaadEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 405 GKLQ---EVVLKSSKVLRADVCVLGIGAVPATGFLRQSGIGL--DSRGFIPVNKMMQTNVPGVFAAGDAVtfplawrnnR 479
Cdd:PRK06327 255 KGVSvayTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLklDERGFIPVDDHCRTNVPNVYAIGDVV---------R 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568996291 480 KvniphWQMAHA---QGRVAAQNMLAQEAEIN--TVPY-LWT----AMFGKSL 522
Cdd:PRK06327 326 G-----PMLAHKaeeEGVAVAERIAGQKGHIDynTIPWvIYTspeiAWVGKTE 373
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
194-467 |
2.00e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 78.42 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 194 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSK--SLDAQPEQLA-LRPKEFFRAYGIEMLTEAQV 270
Cdd:PRK04965 2 SNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHvfSQGQRADDLTrQSAGEFAEQFNLRLFPHTWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 271 VTVDVRNKKVVFKDGfKLEYSKLLLAPGSSPKTLTCKGKdvENVFTIRT-PEDANRVLRLARGRNAVVVGAGFLGMEVAA 349
Cdd:PRK04965 82 TDIDAEAQVVKSQGN-QWQYDKLVLATGASAFVPPIPGR--ELMLTLNSqQEYRAAETQLRDAQRVLVVGGGLIGTELAM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 350 YLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQeVVLKSSKVLRADVCVLGIGA 429
Cdd:PRK04965 159 DLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR-ATLDSGRSIEVDAVIAAAGL 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 568996291 430 VPATGFLRQSGIGLDsRGfIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK04965 238 RPNTALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
197-470 |
3.02e-15 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 78.30 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFSdriVlcTL-DRHlpyDRA-----------KLSKSLdaqpeqlALRPKEFFRAYGIEM 264
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYD---V--TIfEAR---DKAggllrygipefRLPKDI-------VDREVERLLKLGVEI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 265 LTEAQV---VTVDvrnkkvvfkdGFKLEYSKLLLAPG-SSPKTLTCKGKDVENVFT----IRTPEDANRVLRLARGRNAV 336
Cdd:PRK11749 208 RTNTEVgrdITLD----------ELRAGYDAVFIGTGaGLPRFLGIPGENLGGVYSavdfLTRVNQAVADYDLPVGKRVV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 337 VVGAGFLGMEVAAylTEK---AHSVSVV---ELEETP---------------FR------RFLGERVGRALMKmfennrv 389
Cdd:PRK11749 278 VIGGGNTAMDAAR--TAKrlgAESVTIVyrrGREEMPaseeevehakeegveFEwlaapvEILGDEGRVTGVE------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 390 kfYMQTEVSELRAQeGKLQEVVLKSSKVLRADVCVLGIGAVPATGFLR-QSGIGLDSRG-FIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK11749 349 --FVRMELGEPDAS-GRRRVPIEGSEFTLPADLVIKAIGQTPNPLILStTPGLELNRWGtIIADDETGRTSLPGVFAGGD 425
|
...
gi 568996291 468 AVT 470
Cdd:PRK11749 426 IVT 428
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
245-500 |
1.18e-12 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 70.18 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 245 QPeQLALRPKEFFRAYGIEMLTEAQVVTVDVRNKKV-VFKDGFKLEYSKLLLAPGSSPKTLTCKG--------KDVENVF 315
Cdd:PTZ00318 69 RP-ALAKLPNRYLRAVVYDVDFEEKRVKCGVVSKSNnANVNTFSVPYDKLVVAHGARPNTFNIPGveerafflKEVNHAR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 316 TIR---------------TPEDANRVLRLargrnaVVVGAGFLGMEVAAYLTE--------------KAHSVSVVELEET 366
Cdd:PTZ00318 148 GIRkrivqcieraslpttSVEERKRLLHF------VVVGGGPTGVEFAAELADffrddvrnlnpelvEECKVTVLEAGSE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 367 PFRRFlGERVGRALMKMFENNRVKFYMQTEVSELraqegKLQEVVLKSSKVLRADVCV--LGIGAVPATgflRQSGIGLD 444
Cdd:PTZ00318 222 VLGSF-DQALRKYGQRRLRRLGVDIRTKTAVKEV-----LDKEVVLKDGEVIPTGLVVwsTGVGPGPLT---KQLKVDKT 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568996291 445 SRGFIPVNKMMQT-NVPGVFAAGDAVTfplawrNNRKVNIPHWQMAHAQGRVAAQNM 500
Cdd:PTZ00318 293 SRGRISVDDHLRVkPIPNVFALGDCAA------NEERPLPTLAQVASQQGVYLAKEF 343
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
249-468 |
1.67e-12 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 69.84 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 249 LALRPKEFFRAYGI--EMLTEAQVV-------TVDVRNKKVVFKDGFKLEYS--KLLLAPGSSPKTLTCKGKDVEnvfti 317
Cdd:PLN02507 116 LQKKTDEILRLNGIykRLLANAGVKlyegegkIVGPNEVEVTQLDGTKLRYTakHILIATGSRAQRPNIPGKELA----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 318 RTPEDANRVLRLARgrNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERvgRALM-KMFENNRVKFYMQTE 396
Cdd:PLN02507 191 ITSDEALSLEELPK--RAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEM--RAVVaRNLEGRGINLHPRTN 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996291 397 VSELRAQEGKLQeVVLKSSKVLRADVCVLGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDA 468
Cdd:PLN02507 267 LTQLTKTEGGIK-VITDHGEEFVADVVLFATGRAPNTKRlnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
336-467 |
3.03e-12 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 69.03 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 336 VVVGAGFLGMEVAAYLtekaHSVSV-VEL---EETPFRRFLGErVGRALMKMFENNRVKFYMQTEVSELRAQ-EGKLQeV 410
Cdd:PRK06116 171 AVVGAGYIAVEFAGVL----NGLGSeTHLfvrGDAPLRGFDPD-IRETLVEEMEKKGIRLHTNAVPKAVEKNaDGSLT-L 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568996291 411 VLKSSKVLRADVCVLGIGAVPAT-GF-LRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK06116 245 TLEDGETLTVDCLIWAIGREPNTdGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGD 303
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
196-518 |
4.28e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 68.69 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 196 NVLIVGAGAAGLVCAETLRQEGFsdRIVLctLDRHL-----------PydraklSKSL--DAQPEQLALRPKEffraYGI 262
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGM--KVAL--IERGLlggtcvntgcvP------TKTLiaSARAAHLARRAAE----YGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 263 emlTEAQVVTVDVrnKKVV-FKDGFKleysklllapGSSPKTLTCKGKDVENVFTIR---TPEDANRVL---RLARGRNA 335
Cdd:PRK06370 73 ---SVGGPVSVDF--KAVMaRKRRIR----------ARSRHGSEQWLRGLEGVDVFRghaRFESPNTVRvggETLRAKRI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 336 VV-VGA-----GFLGMEVAAYLTekahSVSVVELEETP------------------FRRF--------LGER-------- 375
Cdd:PRK06370 138 FInTGAraaipPIPGLDEVGYLT----NETIFSLDELPehlviigggyiglefaqmFRRFgsevtvieRGPRllpreded 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 376 VGRALMKMFENNRVKFYMQTEVSEL-RAQEGKLQEVVLKS-SKVLRADVCVLGIGAVPATGF--LRQSGIGLDSRGFIPV 451
Cdd:PRK06370 214 VAAAVREILEREGIDVRLNAECIRVeRDGDGIAVGLDCNGgAPEITGSHILVAVGRVPNTDDlgLEAAGVETDARGYIKV 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568996291 452 NKMMQTNVPGVFAAGDavtfplawrnnrkVNIPhWQMAH---AQGRVAAQNML---AQEAEINTVPYlwtAMF 518
Cdd:PRK06370 294 DDQLRTTNPGIYAAGD-------------CNGR-GAFTHtayNDARIVAANLLdggRRKVSDRIVPY---ATY 349
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
197-472 |
5.95e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 67.32 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpYDRaklsksldaQPEQLAL--------R-PKEFFRAyGIEMLTE 267
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGYEVHV----------YDK---------LPEPGGLmlfgipefRiPIERVRE-GVKELEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 268 AQVVTVDvrNKKVVF-------------KDGFKLE-----YSKLLLAPGS-SPKTLTCKGKDVENV-------FTIRTPE 321
Cdd:PRK12770 81 AGVVFHT--RTKVCCgeplheeegdefvERIVSLEelvkkYDAVLIATGTwKSRKLGIPGEDLPGVysaleylFRIRAAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 322 ----DANRVLRLArGRNAVVVGAGFLGMEVA--AYLtEKAHSVSVV---ELEETPFRRFLGERVGRALMKMFEN-NRVKF 391
Cdd:PRK12770 159 lgylPWEKVPPVE-GKKVVVVGAGLTAVDAAleAVL-LGAEKVYLAyrrTINEAPAGKYEIERLIARGVEFLELvTPVRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 392 YMQTEVSELRAQEGKLQ----------EVVLKSSKVLRADVCVLGIGAVPATGFLRQS-GIGLDSRGFIPVNKMMQTNVP 460
Cdd:PRK12770 237 IGEGRVEGVELAKMRLGepdesgrprpVPIPGSEFVLEADTVVFAIGEIPTPPFAKEClGIELNRKGEIVVDEKHMTSRE 316
|
330
....*....|..
gi 568996291 461 GVFAAGDAVTFP 472
Cdd:PRK12770 317 GVFAAGDVVTGP 328
|
|
| Rieske_RO_Alpha_N |
cd03469 |
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ... |
72-158 |
9.81e-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: 62.22 E-value: 9.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFNiSTGDL------ 142
Cdd:cd03469 4 VGHSSELpEPGDYVTLELGGEPLVLVRDrDGEVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYD-LDGKLvgvpre 82
|
90 100
....*....|....*....|
gi 568996291 143 EDFPGLD----SLHKFQVKI 158
Cdd:cd03469 83 EGFPGFDkeklGLRTVPVEE 102
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
255-467 |
1.41e-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: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 255 EFFRAYGieMLTEAQVVTV-DVRNKKVVFKDGFKLEYskLLLAPGSSPKTLTCKGKD--VENVFTIRTPEDANRVLrlar 331
Cdd:TIGR01423 120 TFFLGWG--ALEDKNVVLVrESADPKSAVKERLQAEH--ILLATGSWPQMLGIPGIEhcISSNEAFYLDEPPRRVL---- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 332 grnavVVGAGFLGMEVAAYLTEKAHSVSVVEL--EETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQE 409
Cdd:TIGR01423 192 -----TVGGGFISVEFAGIFNAYKPRGGKVTLcyRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKH 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 410 VVLKSSKVLRADVCVLGIGAVPATGFLR--QSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:TIGR01423 267 VTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
334-414 |
1.57e-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: 60.30 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 334 NAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPfRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKlQEVVLK 413
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL-LPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDG-VVVVLT 78
|
.
gi 568996291 414 S 414
Cdd:pfam00070 79 D 79
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
274-517 |
1.76e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 63.63 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 274 DVRNKKVVFKDGFKLE--YSKLLLAPGSSPKTLTCKG-KD------VENVFTIRTPEdanrvlRLArgrnavVVGAGFLG 344
Cdd:PRK13748 215 DDQTLIVRLNDGGERVvaFDRCLIATGASPAVPPIPGlKEtpywtsTEALVSDTIPE------RLA------VIGSSVVA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 345 MEVAAYLTEKAHSVSVVELEETPFRRflGERVGRALMKMFENNRVKFYMQTEVSELRAQEGklqEVVLKSSK-VLRADVC 423
Cdd:PRK13748 283 LELAQAFARLGSKVTILARSTLFFRE--DPAIGEAVTAAFRAEGIEVLEHTQASQVAHVDG---EFVLTTGHgELRADKL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 424 VLGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPlawrnnrkvniphwQ---MAHAQGRVAAQ 498
Cdd:PRK13748 358 LVATGRAPNTRSLalDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP--------------QfvyVAAAAGTRAAI 423
|
250
....*....|....*....
gi 568996291 499 NMLAQEAEINTvpylwTAM 517
Cdd:PRK13748 424 NMTGGDAALDL-----TAM 437
|
|
| Rieske_NirD_small_Bacillus |
cd03530 |
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ... |
71-165 |
2.66e-10 |
|
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: 57.62 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 71 TVCHVKDLENGQMREVELGWGKVLLVK-DNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDfPGLD 149
Cdd:cd03530 3 DIGALEDIPPRGARKVQTGGGEIAVFRtADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQG-PDEG 81
|
90
....*....|....*.
gi 568996291 150 SLHKFQVKIEKEKVTI 165
Cdd:cd03530 82 CVRTFPVKVEDGRVYL 97
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
284-469 |
3.35e-10 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 62.71 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 284 DGFKLEYSKLLLAPGSSPKTLTCKGKDvenvFTIrtpeDANRVLRLARGRNAVVVGAGFLGMEVAAYLTEKAHSVSVVEL 363
Cdd:PTZ00058 197 DGQVIEGKNILIAVGNKPIFPDVKGKE----FTI----SSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 364 EETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSEL-RAQEGKLQEVVLKSSKVLRADVCVLGIGAVPATGFLRQSGIG 442
Cdd:PTZ00058 269 GNRLLRKF-DETIINELENDMKKNNINIITHANVEEIeKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALN 347
|
170 180
....*....|....*....|....*...
gi 568996291 443 -LDSRGFIPVNKMMQTNVPGVFAAGDAV 469
Cdd:PTZ00058 348 iKTPKGYIKVDDNQRTSVKHIYAVGDCC 375
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
294-496 |
4.29e-09 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 59.10 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 294 LLAPGSSPKTLTCKGKDVENVFTIRT-------PEdanrvlRLargrnaVVVGAGFLGMEVAAYLTEKAHSVSVV----- 361
Cdd:PRK07845 144 LIATGASPRILPTAEPDGERILTWRQlydldelPE------HL------IVVGSGVTGAEFASAYTELGVKVTLVssrdr 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 362 ----------ELEETPFRRflgervgRAlMKMFENNRVKfymqtevSELRAQEGklQEVVLKSSKVLRADVCVLGIGAVP 431
Cdd:PRK07845 212 vlpgedadaaEVLEEVFAR-------RG-MTVLKRSRAE-------SVERTGDG--VVVTLTDGRTVEGSHALMAVGSVP 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 432 AT---GfLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVT--FPLAwrnnrkvniphwQMAHAQGRVA 496
Cdd:PRK07845 275 NTaglG-LEEAGVELTPSGHITVDRVSRTSVPGIYAAGD-CTgvLPLA------------SVAAMQGRIA 330
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
337-467 |
1.14e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 57.45 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 337 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlgERVGRALMKMF-ENNRVKFYMQTEVSELRAQEGKLqeVVLKSS 415
Cdd:PRK07251 162 IIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE--EPSVAALAKQYmEEDGITFLLNAHTTEVKNDGDQV--LVVTED 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568996291 416 KVLRADVCVLGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK07251 238 ETYRFDALLYATGRKPNTEplGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
187-497 |
2.42e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 57.05 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 187 PSAGHSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpydraklsksLDAQPEqlalrPKEFFRaYGI---- 262
Cdd:PRK12814 186 PERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTI-------------------FDANEQ-----AGGMMR-YGIprfr 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 263 --EMLTEAQV-----VTVDVRNKKVVFKD----GFKLEYSKLLLAPGSS-PKTLTCKGKDVENVFT-IRTPEDANRVLRL 329
Cdd:PRK12814 241 lpESVIDADIaplraMGAEFRFNTVFGRDitleELQKEFDAVLLAVGAQkASKMGIPGEELPGVISgIDFLRNVALGTAL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 330 ARGRNAVVVGAGFLGMEVA-AYLTEKAHSVSVV---ELEETPFRRflgERVGRALMkmfENNRVKFYM----------QT 395
Cdd:PRK12814 321 HPGKKVVVIGGGNTAIDAArTALRLGAESVTILyrrTREEMPANR---AEIEEALA---EGVSLRELAapvsiersegGL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 396 EVSELRAQEGKLQE------VVLKSSK-VLRADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNVPGVFAAGD 467
Cdd:PRK12814 395 ELTAIKMQQGEPDEsgrrrpVPVEGSEfTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPeTLQTSVAGVFAGGD 474
|
330 340 350
....*....|....*....|....*....|.
gi 568996291 468 AVTFP-LAWRnnrkvniphwqmAHAQGRVAA 497
Cdd:PRK12814 475 CVTGAdIAIN------------AVEQGKRAA 493
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
228-518 |
2.48e-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: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 228 DRHLPYDRAKLSKSLDAQPEQL------ALRPKE--FFRAYGieMLTEAQVVTVDVRNKKVVFKDGfkleySKLLLAPGS 299
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLnwgyrvALREKKvkYENAYA--EFVDKHRIKATNKKGKEKIYSA-----ERFLIATGE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 300 SPKTLTCKGKD-----VENVFTIrtPEDANRVLrlargrnavVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFlGE 374
Cdd:TIGR01438 154 RPRYPGIPGAKelcitSDDLFSL--PYCPGKTL---------VVGASYVALECAGFLAGIGLDVTVM-VRSILLRGF-DQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 375 RVGRALMKMFENNRVKFYMQTEVSELRAQEGKlqeVVLKSSKVLRA-----DVCVLGIGAVPATgflrqSGIGLDSRGF- 448
Cdd:TIGR01438 221 DCANKVGEHMEEHGVKFKRQFVPIKVEQIEAK---VLVEFTDSTNGieeeyDTVLLAIGRDACT-----RKLNLENVGVk 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568996291 449 -------IPVNKMMQTNVPGVFAAGDAVtfplawrNNRKVNIPhwqMAHAQGRVAAQNMLAQEAEINTVPYLWTAMF 518
Cdd:TIGR01438 293 inkktgkIPADEEEQTNVPYIYAVGDIL-------EDKPELTP---VAIQAGRLLAQRLFKGSTVICDYENVPTTVF 359
|
|
| Rieske_T4moC |
cd03474 |
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ... |
72-166 |
2.72e-08 |
|
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.
Pssm-ID: 239556 [Multi-domain] Cd Length: 108 Bit Score: 51.95 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 72 VCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDfPGLDS 150
Cdd:cd03474 4 VCSLDDVWEGEMELVDVDGEEVLLVaPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGLN-PRDCR 82
|
90
....*....|....*.
gi 568996291 151 LHKFQVKIEKEKVTIR 166
Cdd:cd03474 83 LARYPVKVEGGDILVD 98
|
|
| HcaE |
COG4638 |
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ... |
72-156 |
3.69e-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: 55.38 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN-----ISTGDLED 144
Cdd:COG4638 30 VGHSSELpEPGDYLTRTILGEPVVLVRDkDGEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDldgrlVGIPHMEG 109
|
90
....*....|....*.
gi 568996291 145 FPGLD----SLHKFQV 156
Cdd:COG4638 110 FPDFDparaGLRSVPV 125
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
318-501 |
5.22e-08 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 55.73 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 318 RTPEDanrVLRLAR-GRNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRF---LGERVGRALMKmfennRVKFYM 393
Cdd:PRK07846 154 HTSDT---IMRLPElPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLdddISERFTELASK-----RWDVRL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 394 QTEVSELRAQEGKLqEVVLKSSKVLRADVCVLGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDaVTF 471
Cdd:PRK07846 226 GRNVVGVSQDGSGV-TLRLDDGSTVEADVLLVATGRVPNGDLLdaAAAGVDVDEDGRVVVDEYQRTSAEGVFALGD-VSS 303
|
170 180 190
....*....|....*....|....*....|...
gi 568996291 472 PlawrnnrkvniphWQMAH---AQGRVAAQNML 501
Cdd:PRK07846 304 P-------------YQLKHvanHEARVVQHNLL 323
|
|
| Reductase_C |
pfam14759 |
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ... |
512-562 |
1.18e-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: 49.48 E-value: 1.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568996291 512 YLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKSDEVIAVASMN 562
Cdd:pfam14759 1 WFWSDQYDLKLQIAGLPTGADEVVLRGDPEDGAFSVFYLRDGRLVAVDAVN 51
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
163-500 |
1.31e-07 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 54.50 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 163 VTIRASKQAL-QLQRRTKVMAkcisPSAGHSSSTNVLIVGAGAAGLVCAETLRQEGFSdrivlCTLdrhlpydraklsks 241
Cdd:PRK12771 109 VGINAVERFLgDYAIANGWKF----PAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHA-----VTI-------------- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 242 LDAQPeQLA--LRpkeffraYGI-------EML-TEAQVVT---VDVRNKKVVFKD--GFKLE--YSKLLLAPG-SSPKT 303
Cdd:PRK12771 166 FEAGP-KLGgmMR-------YGIpayrlprEVLdAEIQRILdlgVEVRLGVRVGEDitLEQLEgeFDAVFVAIGaQLGKR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 304 LTCKGKDVENVFT----IRTPEDANRVLRlarGRNAVVVGAGFLGMEVAAylTEK---AHSVSVV-------------EL 363
Cdd:PRK12771 238 LPIPGEDAAGVLDavdfLRAVGEGEPPFL---GKRVVVIGGGNTAMDAAR--TARrlgAEEVTIVyrrtredmpahdeEI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 364 EE------------TPfRRFLGERVGRALMKMfennrVKFYMQTEVSELRAQEGKLQEVVLKsskvlrADVCVLGIGAVP 431
Cdd:PRK12771 313 EEalregveinwlrTP-VEIEGDENGATGLRV-----ITVEKMELDEDGRPSPVTGEEETLE------ADLVVLAIGQDI 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 432 ATGFLRQSGIGLDSRGFIPVNKM-MQTNVPGVFAAGDAVTFPlawrnnRKVNiphwqMAHAQGRVAAQNM 500
Cdd:PRK12771 381 DSAGLESVPGVEVGRGVVQVDPNfMMTGRPGVFAGGDMVPGP------RTVT-----TAIGHGKKAARNI 439
|
|
| PRK09965 |
PRK09965 |
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional |
72-165 |
1.95e-07 |
|
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
Pssm-ID: 170182 [Multi-domain] Cd Length: 106 Bit Score: 49.39 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 72 VCHVKDLENGQMREVELGwGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLS-RGRVRCPWHGACFNISTGDLEDFPGLDS 150
Cdd:PRK09965 6 ACPVADLPEGEALRVDTS-PVIALFNVGGEFYAIDDRCSHGNASLSEGYLEdDATVECPLHAASFCLRTGKALCLPATDP 84
|
90
....*....|....*
gi 568996291 151 LHKFQVKIEKEKVTI 165
Cdd:PRK09965 85 LRTYPVHVEGGDIFI 99
|
|
| PobA |
COG5749 |
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]; |
72-149 |
2.46e-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: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 72 VCHVKDLENGQMREVELgWGK-VLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiSTGDLEDFPGLD 149
Cdd:COG5749 23 VAPSEDLKPNKPKPVTL-LGEpLVIWRDsDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYHGWQFD-GDGKCVHIPQLP 100
|
|
| Rieske_RO_Alpha_VanA_DdmC |
cd03532 |
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ... |
100-136 |
2.95e-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: 2.95e-07
10 20 30
....*....|....*....|....*....|....*..
gi 568996291 100 GEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN 136
Cdd:cd03532 37 GRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFD 73
|
|
| QcrA/PetC |
COG0723 |
Rieske Fe-S protein [Energy production and conversion]; |
75-165 |
5.31e-07 |
|
Rieske Fe-S protein [Energy production and conversion];
Pssm-ID: 440487 [Multi-domain] Cd Length: 118 Bit Score: 48.46 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 75 VKDLENGQMREVELGWGKVLLVK----DNGEFHALGHKCPHYGAPlVKGVLSRGRVRCPWHGACFNIS----TGdledfP 146
Cdd:COG0723 23 LSDLPPGEGKVVEWRGKPVFVVRtpvrGDGEIVAVSAICTHLGCP-VTWNADEGGFDCPCHGSRFDPDgrvlKG-----P 96
|
90
....*....|....*....
gi 568996291 147 GLDSLHKFQVKIEKEKVTI 165
Cdd:COG0723 97 APRPLPVPPLEVDDDKLLI 115
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
427-472 |
5.58e-07 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 52.47 E-value: 5.58e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568996291 427 IGAVPATGFLRQSgIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFP 472
Cdd:PRK15317 445 IGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVP 489
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
197-472 |
2.43e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 50.54 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFsDRIVLCTLDR------------HLPYDraklskSLDaqpeqlalRPKEFFRAYGIEM 264
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKpggvmrygipsyRLPDE------ALD--------KDIAFIEALGVKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 265 LTEAQVVtvdvrnKKVVFKDgFKLEYSKLLLAPG-SSPKTLTCKGKDVENVFtirtpeDANRVLRLARG----------- 332
Cdd:PRK13984 351 HLNTRVG------KDIPLEE-LREKHDAVFLSTGfTLGRSTRIPGTDHPDVI------QALPLLREIRDylrgegpkpki 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 333 -RNAVVVGAGFLGMEVAAYLTE------KAHSVSVVELEET---------PFRRFLGERV----GRALMK-MFENNRVKF 391
Cdd:PRK13984 418 pRSLVVIGGGNVAMDIARSMARlqkmeyGEVNVKVTSLERTfeempadmeEIEEGLEEGVviypGWGPMEvVIENDKVKG 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 392 YMQTEVSELRAQEGKLQEVVLKSSK-VLRADVCVLGIGAVPATGFLRQSgigLDS-----RGFIPVNKMMQTNVPGVFAA 465
Cdd:PRK13984 498 VKFKKCVEVFDEEGRFNPKFDESDQiIVEADMVVEAIGQAPDYSYLPEE---LKSklefvRGRILTNEYGQTSIPWLFAG 574
|
....*..
gi 568996291 466 GDAVTFP 472
Cdd:PRK13984 575 GDIVHGP 581
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
271-468 |
7.75e-06 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 49.14 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 271 VTVDVRNKKVVFKDGFKLEYS-------KLLLAPGSSPKTLTCKGKDVENVFTirtpedANRVLRLARGRNAV-VVGAGF 342
Cdd:PTZ00153 249 VQVIYERGHIVDKNTIKSEKSgkefkvkNIIIATGSTPNIPDNIEVDQKSVFT------SDTAVKLEGLQNYMgIVGMGI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 343 LGMEVAAYLTekAHSVSVVELEETP-FRRFLGERVGRALMKMFENNR-VKFYMQTEVSELRAQEGKlQEVVLKSS----- 415
Cdd:PTZ00153 323 IGLEFMDIYT--ALGSEVVSFEYSPqLLPLLDADVAKYFERVFLKSKpVRVHLNTLIEYVRAGKGN-QPVIIGHSerqtg 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568996291 416 ------------KVLRADVCVLGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTN------VPGVFAAGDA 468
Cdd:PTZ00153 400 esdgpkknmndiKETYVDSCLVATGRKPNT-----NNLGLDKlkiqmkRGFVSVDEHLRVLredqevYDNIFCIGDA 471
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
331-466 |
7.89e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 47.99 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 331 RGRNAVVVGAGFLGMEVAAYLTEKAHSVSVV------ELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQE 404
Cdd:pfam13738 154 AGQKVVVIGGYNSAVDAALELVRKGARVTVLyrgsewEDRDSDPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKEITEVD 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568996291 405 GklqEVVLKSS---KVLRADVCVLGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNVPGVFAAG 466
Cdd:pfam13738 234 V---SYKVHTEdgrKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEeTESTNVPGLFLAG 296
|
|
| Rieske_RO_Alpha_OMO_CARDO |
cd03548 |
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ... |
76-144 |
1.58e-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: 1.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996291 76 KDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGV--LSRGRVRCPWHGACFNISTGDLED 144
Cdd:cd03548 22 HELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPecFTKGTITCWYHGWTYRLDDGKLVT 92
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
197-470 |
1.91e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 47.32 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFSDRI--VLCTLDRHLPYdraklsksldAQPEqlaLR-PKEFFRAYGIEMLTEAQV--V 271
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIfeALHEPGGVLVY----------GIPE---FRlPKETVVKKEIENIKKLGVkiE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 272 TVDVRNKKVVFKDGFKLE-YSKLLLAPGSS-PKTLTCKGKDVENVFTirtpedANRVLR---------------LARGRN 334
Cdd:PRK12831 210 TNVVVGKTVTIDELLEEEgFDAVFIGSGAGlPKFMGIPGENLNGVFS------ANEFLTrvnlmkaykpeydtpIKVGKK 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 335 AVVVGAGFLGMEVAAY---LTEKAHSVSVVELEETPFRRflgERVGRAL-----MKMF---------ENNRVKfYMQTEV 397
Cdd:PRK12831 284 VAVVGGGNVAMDAARTalrLGAEVHIVYRRSEEELPARV---EEVHHAKeegviFDLLtnpveilgdENGWVK-GMKCIK 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568996291 398 SEL--RAQEGKLQEVVLKSSK-VLRADVCVLGIGAVPATGFLRQS-GIGLDSRGFIPVNK-MMQTNVPGVFAAGDAVT 470
Cdd:PRK12831 360 MELgePDASGRRRPVEIEGSEfVLEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADEeTGLTSKEGVFAGGDAVT 437
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
337-467 |
3.79e-05 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 46.55 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 337 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRfLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQevVLKSSK 416
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHENQVQ--VHSEHA 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568996291 417 VLRADVCVLGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK08010 240 QLAVDALLIASGRQPATASLhpENAGIAVNERGAIVVDKYLHTTADNIWAMGD 292
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
181-501 |
1.63e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 44.74 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 181 MAKCISPSAGHSSSTN--VLIVGAGAAGLVCAETLRQEGFSDRIvlctLDRH----------LPydRAKLSKSLDAqpeq 248
Cdd:PRK12769 312 LAKGWRPDLSQVTKSDkrVAIIGAGPAGLACADVLARNGVAVTV----YDRHpeigglltfgIP--AFKLDKSLLA---- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 249 lalRPKEFFRAYGIEMLTEAQVvtvdvrnKKVVFKDGFKLEYSKLLLAPGS--SPKTltckGKDVENV--------FTIR 318
Cdd:PRK12769 382 ---RRREIFSAMGIEFELNCEV-------GKDISLESLLEDYDAVFVGVGTyrSMKA----GLPNEDApgvydalpFLIA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 319 T-------PEDANRVLRLARGRNAVVVGAGFLGME-VAAYLTEKAHSV-------------SVVEL----EETPFRRFLG 373
Cdd:PRK12769 448 NtkqvmglEELPEEPFINTAGLNVVVLGGGDTAMDcVRTALRHGASNVtcayrrdeanmpgSKKEVknarEEGANFEFNV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 374 ERVGRALMKMFENNRVKFyMQTEVSELRAQeGKLQEVVLKSSK-VLRADVCVLGIGAVPAT-GFLRQSGIGLDSRGFI-- 449
Cdd:PRK12769 528 QPVALELNEQGHVCGIRF-LRTRLGEPDAQ-GRRRPVPIPGSEfVMPADAVIMAFGFNPHGmPWLESHGVTVDKWGRIia 605
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568996291 450 PVNKMM--QTNVPGVFAAGDAVtfplawRNNRKVniphwQMAHAQGRVAAQNML 501
Cdd:PRK12769 606 DVESQYryQTSNPKIFAGGDAV------RGADLV-----VTAMAEGRHAAQGII 648
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
196-285 |
2.60e-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: 39.88 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 196 NVLIVGAGAAGLVCAETLRQEGfSDRIVLCTLDRHLPYDRAKLSKSLdaqpeqlalrpKEFFRAYGIEMLTEAQV--VTV 273
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLG-SKVTVVERRDRLLPGFDPEIAKIL-----------QEKLEKNGIEFLLNTTVeaIEG 68
|
90
....*....|..
gi 568996291 274 DVRNKKVVFKDG 285
Cdd:pfam00070 69 NGDGVVVVLTDG 80
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
187-470 |
2.64e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 43.96 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 187 PSAGHSSSTNVLIVGAGAAGLVCAETLRQEGFsDRIVLCTLdrHLPYDRAKLSKSLDAQPEQLALRPKEFFRAYGIEMLT 266
Cdd:PRK12778 424 PEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGY-DVTVFEAL--HEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFET 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 267 E---AQVVTVDVrnkkvVFKDGFKleysKLLLAPGSS-PKTLTCKGKDVENVFTirTPEDANRV-----------LRLAR 331
Cdd:PRK12778 501 DvivGKTITIEE-----LEEEGFK----GIFIASGAGlPNFMNIPGENSNGVMS--SNEYLTRVnlmdaaspdsdTPIKF 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 332 GRNAVVVGAGFLGMEVAAylTEK---AHSVSVV---ELEETPFRRflgERVGRALMK----MFENNRVKfYMQTE---VS 398
Cdd:PRK12778 570 GKKVAVVGGGNTAMDSAR--TAKrlgAERVTIVyrrSEEEMPARL---EEVKHAKEEgiefLTLHNPIE-YLADEkgwVK 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 399 ELRAQEGKLQE---------VVLKSSKV-LRADVCVLGIGAVPATGFLRQ-SGIGLDSRGFIPVNKMMQTNVPGVFAAGD 467
Cdd:PRK12778 644 QVVLQKMELGEpdasgrrrpVAIPGSTFtVDVDLVIVSVGVSPNPLVPSSiPGLELNRKGTIVVDEEMQSSIPGIYAGGD 723
|
...
gi 568996291 468 AVT 470
Cdd:PRK12778 724 IVR 726
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
199-230 |
4.35e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 38.67 E-value: 4.35e-04
10 20 30
....*....|....*....|....*....|..
gi 568996291 199 IVGAGAAGLVCAETLRQEGFsdRIVLctLDRH 230
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGF--RVLV--LEKR 28
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
193-219 |
4.95e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 42.56 E-value: 4.95e-04
10 20
....*....|....*....|....*..
gi 568996291 193 SSTNVLIVGAGAAGLVCAETLRQEGFS 219
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHE 28
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
197-222 |
5.35e-04 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 42.60 E-value: 5.35e-04
10 20 30
....*....|....*....|....*....|...
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGF-------SDRI 222
Cdd:COG1231 10 VVIVGAGLAGLAAARELRKAGLdvtvleaRDRV 42
|
|
| Rieske_RO_Alpha_PaO |
cd03480 |
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ... |
56-146 |
9.37e-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: 39.61 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 56 PTPQPYPSPQDCVEA--TVCHVKDLENGQMRevelgwGKVLLVKD--------NGEFHALGHKCPHYGAPLVKGVLSR-G 124
Cdd:cd03480 3 PAGGSDSDKFDWREVwyPVAYVEDLDPSRPT------PFTLLGRDlviwwdrnSQQWRAFDDQCPHRLAPLSEGRIDEeG 76
|
90 100
....*....|....*....|..
gi 568996291 125 RVRCPWHGACFNiSTGDLEDFP 146
Cdd:cd03480 77 CLECPYHGWSFD-GSGSCQRIP 97
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
336-518 |
1.13e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 41.73 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 336 VVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQeVVLKSS 415
Cdd:PTZ00052 186 LIVGASYIGLETAGFLNELGFDVTVA-VRSIPLRGF-DRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIK-VLFSDG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 416 KVLRADVCVLGIGAVPATGFLRQSGIGL---DSRGFIPVNKMmqTNVPGVFAAGDAVtfplawrnnrkVNIPHWQ-MAHA 491
Cdd:PTZ00052 263 TTELFDTVLYATGRKPDIKGLNLNAIGVhvnKSNKIIAPNDC--TNIPNIFAVGDVV-----------EGRPELTpVAIK 329
|
170 180
....*....|....*....|....*..
gi 568996291 492 QGRVAAQNMLAQEAEINTVPYLWTAMF 518
Cdd:PTZ00052 330 AGILLARRLFKQSNEFIDYTFIPTTIF 356
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
389-468 |
1.57e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 41.38 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 389 VKF--YMQTEVSElrAQEGKLQ----EVVLKSSKVLRADVCVLGIGAVPATG---FLRQSGIGLDSRGFI----PVNKMM 455
Cdd:COG1148 365 VRFirGRVAEIEE--DEGGKLVvtveDTLLGEPVEIEADLVVLATGMVPSEDneeLAKLLKLPLDQDGFFleahPKLRPV 442
|
90
....*....|...
gi 568996291 456 QTNVPGVFAAGDA 468
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 |
1.60e-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: 1.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996291 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 |
1.97e-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: 39.15 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568996291 99 NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiSTGDLEDFPGL--DSLHKFQVKI 158
Cdd:cd03479 54 SGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFD-VDGQCLEMPSEppDSQLKQKVRQ 114
|
|
| SfcA |
COG0281 |
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ... |
197-230 |
4.32e-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: 4.32e-03
10 20 30
....*....|....*....|....*....|....*
gi 568996291 197 VLIVGAGAAGLVCAETLRQEGFS-DRIVLCtlDRH 230
Cdd:COG0281 194 IVINGAGAAGIAIARLLVAAGLSeENIIMV--DSK 226
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
198-219 |
5.60e-03 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 39.26 E-value: 5.60e-03
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
195-466 |
7.40e-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: 39.08 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 195 TNVLIVGAGAAGLVCAETLRQEGFSDRIvlctLD---------RHLPYDRAKL----------SKSLDAQPEQLALRP-- 253
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVV----LEkaddvggtwRDNRYPGLRLdtpshlyslpFFPNWSDDPDFPTGDei 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 254 KEFFRAY----GIE--MLTEAQVVTVDVRNKK----VVFKDGFKLEYSKLLLAPG--SSPKTLTCKGKDvenVFTIRT-- 319
Cdd:COG2072 83 LAYLEAYadkfGLRrpIRFGTEVTSARWDEADgrwtVTTDDGETLTARFVVVATGplSRPKIPDIPGLE---DFAGEQlh 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 320 PEDANRVLRLArGRNAVVVGAGFLGMEVAAYLTEKAHSVSVV--------------------------ELEETPFRRFLG 373
Cdd:COG2072 160 SADWRNPVDLA-GKRVLVVGTGASAVQIAPELARVAAHVTVFqrtppwvlprpnydpergrpanylglEAPPALNRRDAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996291 374 ERVGRALMKMFENNRVKFYMQTEV---------SELR--AQEGKLQ------------EVVLKSSKVLRADVCVLGIGAV 430
Cdd:COG2072 239 AWLRRLLRAQVKDPELGLLTPDYPpgckrpllsTDYYeaLRRGNVElvtggieritedGVVFADGTEHEVDVIVWATGFR 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 568996291 431 PATGFLRQSGI-GLDSRGFIPVNK-MMQTNVPGVFAAG 466
Cdd:COG2072 319 ADLPWLAPLDVrGRDGRSGPRAYLgVVVPGFPNLFFLG 356
|
|
| |
