|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
193-561 |
8.57e-103 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 317.08 E-value: 8.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 193 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSKSL--DAQPEQLALRPKEFFRAYGIEMLTEAQVV 270
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLagETDEEDLLLRPADFYEENGIDLRLGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 271 TVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDIENVFTIRTPEDANRVL-RLARGRNAVVVGAGFLGMEVAAY 349
Cdd:COG1251 81 AIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRaALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 350 LTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAqEGKLQEVVLKSSKVLRADVCVVGIGAV 429
Cdd:COG1251 161 LRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 430 PATGFLRQSGIGLDsRGfIPVNKMMQTNIPGVFAAGDAVTFPLAWRNNRKVniPHWQMAHAQGRVAAQNMLAQEAEIN-T 508
Cdd:COG1251 240 PNTELARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVL--ELVAPAYEQARVAAANLAGGPAAYEgS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958665283 509 VPYLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMN 561
Cdd:COG1251 316 VPSTKLKVFGVDVASAGDAEGDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVG 368
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
214-529 |
2.60e-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: 263.98 E-value: 2.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 214 QEGFSDRIVLctLDR--HLPYDRAKLSKSL---DAQPEQLALRPKEFFRAYGIEMLTEAQVVTVDVRNKKVVFKDGFKLE 288
Cdd:COG0446 1 RLGPDAEITV--IEKgpHHSYQPCGLPYYVgggIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 289 YSKLLLAPGSSPKTLTCKGKDIENVFTIRTPEDANRV---LRLARGRNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEET 365
Cdd:COG0446 79 YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALreaLKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 366 PFRRFLGErVGRALMKMFENNRVKFYMQTEVSELRAQEGklQEVVLKSSKVLRADVCVVGIGAVPATGFLRQSGIGLDSR 445
Cdd:COG0446 159 LLGVLDPE-MAALLEEELREHGVELRLGETVVAIDGDDK--VAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 446 GFIPVNKMMQTNIPGVFAAGDAVTFPLAwRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEINTVPYLWTAMFGksLRYAG 525
Cdd:COG0446 236 GWIKVDETLQTSDPDVYAAGDCAEVPHP-VTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFD--LCIAS 312
|
....
gi 1958665283 526 YGEG 529
Cdd:COG0446 313 TGTG 316
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
194-492 |
4.01e-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: 4.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 194 TNVLIVGAGAAGLVCAETLRQEGFsdRIVLCTLDRHLPYDRAKLSKSLDAQPEQ--LALRPKEFFRAY---------GIE 262
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGG--KVTLIEDEGTCPYGGCVLSKALLGAAEApeIASLWADLYKRKeevvkklnnGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 263 MLTEAQVVTVDVRNKKVVFK-----DGFKLEYSKLLLAPGSSPKTLTCKGKDIENVFTIRTPEDANRVLRLARGRNAVVV 337
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKRVVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 338 GAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLqEVVLKSSKVL 417
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-DEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGV-EVILKDGTEI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958665283 418 RADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGDAvtfplawrnnRKVNIPHWQMAHAQG 492
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 |
8.47e-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: 178.20 E-value: 8.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 70 ATVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIGTGDLEDFPGLD 149
Cdd:cd03478 1 AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALD 80
|
90
....*....|....
gi 1958665283 150 SLHKFQVKIEKEKV 163
Cdd:cd03478 81 SLPCYEVEVEDGRV 94
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
193-584 |
3.41e-52 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 183.97 E-value: 3.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 193 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSKS--LDAQPEQLALRPKEFFRAYGIEMLTEAQVV 270
Cdd:PRK09754 3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSmlLEDSPQLQQVLPANWWQENNVHLHSGVTIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 271 TVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDIENVFTIRTPEDANRvLR--LARGRNAVVVGAGFLGMEVAA 348
Cdd:PRK09754 83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAAR-LRevLQPERSVVIVGAGTIGLELAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 349 YLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVseLRAQEGKLQEVVLKSSKVLRADVCVVGIGA 428
Cdd:PRK09754 162 SATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAI--EHVVDGEKVELTLQSGETLQADVVIYGIGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 429 VPATGFLRQSgiGLDSRGFIPVNKMMQTNIPGVFAAGDAVT--FPLAWRNNRKVniphWQMAHAQGRVAAQNMLAQEAEI 506
Cdd:PRK09754 240 SANDQLAREA--NLDTANGIVIDEACRTCDPAIFAGGDVAItrLDNGALHRCES----WENANNQAQIAAAAMLGLPLPL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958665283 507 NTVPYLWTAMFGKSLRYAGYGEGfDDVIIQGDLEELKFVAFYTKGDEVIAVASMNYDPIVSKVAEVLASGRAIRKREV 584
Cdd:PRK09754 314 LPPPWFWSDQYSDNLQFIGDMRG-DDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLL 390
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
194-511 |
2.74e-39 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 148.36 E-value: 2.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 194 TNVLIVGAGAAGLVCAETLRQEGFSD-RIVLctLDRH--------LPYDrakLSKSLDaqPEQLALRPKEFFRAYGIEML 264
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDaEVTL--IDPNpyhlfqplLPEV---AAGTLS--PDDIAIPLRELLRRAGVRFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 265 TeAQVVTVDVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGKDiENVFTIRTPEDA----NRVLRL------ARGRNA 334
Cdd:COG1252 75 Q-GEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDAlalrERLLAAferaerRRLLTI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 335 VVVGAGFLGMEVAAYLTEKAH-------------SVSVVELEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRA 401
Cdd:COG1252 153 VVVGGGPTGVELAGELAELLRkllrypgidpdkvRITLVEAGPRILPGL-GEKLSEAAEKELEKRGVEVHTGTRVTEVDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 402 qegklQEVVLKSSKVLRADvCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQT-NIPGVFAAGDAVTFPLAwrnnrkv 480
Cdd:COG1252 232 -----DGVTLEDGEEIPAD-TVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDP------- 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958665283 481 nIPHW-----QMAHAQGRVAAQNMLAQEAEINTVPY 511
Cdd:COG1252 299 -DGKPvpktaQAAVQQAKVLAKNIAALLRGKPLKPF 333
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
194-498 |
2.12e-35 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 135.25 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 194 TNVLIVGAGAAGLVCAETLRQEGFSdrIVLctLDRHLPYDRAKLSKSLD--------AQPEQLALRPKEFFRAYGIEMLT 265
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLK--TLV--IEGGEPGGQLATTKEIEnypgfpegISGPELAERLREQAERFGAEILL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 266 EaQVVTVDV--RNKKVVFKDGFKLEYSKLLLAPGSSPKTLTCKGkdiENVFTIR-----TPEDANrvlrLARGRNAVVVG 338
Cdd:COG0492 77 E-EVTSVDKddGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPG---EEEFEGRgvsycATCDGF----FFRGKDVVVVG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 339 AGFLGMEVAAYLTEKAHSVSVVeleetpFRR--FLGERVgrALMKMFENNRVKFYMQTEVSELRAqEGKLQEVVLKSSK- 415
Cdd:COG0492 149 GGDSALEEALYLTKFASKVTLI------HRRdeLRASKI--LVERLRANPKIEVLWNTEVTEIEG-DGRVEGVTLKNVKt 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 416 ----VLRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGDAVTFplawrnnrkvniPHWQMAHA- 490
Cdd:COG0492 220 geekELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY------------KYRQAATAa 287
|
....*....
gi 1958665283 491 -QGRVAAQN 498
Cdd:COG0492 288 gEGAIAALS 296
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
194-489 |
1.17e-34 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 136.45 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 194 TNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRH-------LPYdraKLSKSLDAQPEQLALRPKEFFRAYGIEMLTE 266
Cdd:PRK13512 2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDmsfancaLPY---YIGEVVEDRKYALAYTPEKFYDRKQITVKTY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 267 AQVVTVDVRNKKVVFKD-----GFKLEYSKLLLAPGSSPKTLtckGKDIENVFTIRTPEDANRV---LRLARGRNAVVVG 338
Cdd:PRK13512 79 HEVIAINDERQTVTVLNrktneQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIdqfIKANQVDKALVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 339 AGFLGMEVAAYLTEKAHSVSVVElEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEgklqeVVLKSSKVLR 418
Cdd:PRK13512 156 AGYISLEVLENLYERGLHPTLIH-RSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNE-----VTFKSGKVEH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 419 ADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGDAVT-----------FPLAWRNNRKVNIPHWQM 487
Cdd:PRK13512 230 YDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITshyrhvdlpasVPLAWGAHRAASIVAEQI 309
|
..
gi 1958665283 488 AH 489
Cdd:PRK13512 310 AG 311
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
196-499 |
7.99e-32 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 128.23 E-value: 7.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFSDRIVL-----------CTLdrhlPYDRAKLSKSldaqPEQLALRPKEFFRAYGIEML 264
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNKELEITVyektdivsfgaCGL----PYFVGGFFDD----PNTMIARTPEEFIKSGIDVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 265 TEAQVVTVDVRNKKVVFKDG-----FKLEYSKLLLAPGSSPKTLTCKGKDIENVFTIRTPEDANRV---LRLARGRNAVV 336
Cdd:PRK09564 75 TEHEVVKVDAKNKTITVKNLktgsiFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALkelLKDEEIKNIVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 337 VGAGFLGMEVAAYLTEKAHSVSVVELEEtpfrRFLGERVGRALMKMFEN----NRVKFYMQTEVSELRAqEGKLQEVVLK 412
Cdd:PRK09564 155 IGAGFIGLEAVEAAKHLGKNVRIIQLED----RILPDSFDKEITDVMEEelreNGVELHLNEFVKSLIG-EDKVEGVVTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 413 SSKVlRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGD-AVTFPLAwrNNRKVNIPHWQMAHAQ 491
Cdd:PRK09564 230 KGEY-EADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcATIYNIV--SNKNVYVPLATTANKL 306
|
....*...
gi 1958665283 492 GRVAAQNM 499
Cdd:PRK09564 307 GRMVGENL 314
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
196-511 |
3.28e-29 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 120.96 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFsdRIVL---------CTLD------------------RHLP----------YDRAKLS 238
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGL--KVALvekgrlggtCLNVgcipskallhaaevaheaRHAAefgisagapsVDWAALM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 239 KSLDAQPEQLALRPKEFFRAYGIEMLT-EAQVV---TVDVRNKKVvfkdgfkLEYSKLLLAPGSSPKTLTCKGKDIENVF 314
Cdd:COG1249 84 ARKDKVVDRLRGGVEELLKKNGVDVIRgRARFVdphTVEVTGGET-------LTADHIVIATGSRPRVPPIPGLDEVRVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 315 TIRTpedanrVLRLAR-GRNAVVVGAGFLGMEVAAYL----TEkahsVSVVELEETPFRRFlGERVGRALMKMFENNRVK 389
Cdd:COG1249 157 TSDE------ALELEElPKSLVVIGGGYIGLEFAQIFarlgSE----VTLVERGDRLLPGE-DPEISEALEKALEKEGID 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 390 FYMQTEVSELRAQEGKLqEVVLKS---SKVLRADVCVVGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNIPGVFAA 464
Cdd:COG1249 226 ILTGAKVTSVEKTGDGV-TVTLEDgggEEAVEADKVLVATGRRPNTDglGLEAAGVELDERGGIKVDEYLRTSVPGIYAI 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958665283 465 GDAVTFP-LAwrnnrkvnipHwqMAHAQGRVAAQNMLAQEAEI---NTVPY 511
Cdd:COG1249 305 GDVTGGPqLA----------H--VASAEGRVAAENILGKKPRPvdyRAIPS 343
|
|
| NirD |
COG2146 |
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ... |
69-166 |
2.91e-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: 108.78 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 69 EATVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIGTGDLEDFPGL 148
Cdd:COG2146 3 EVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLGGPAT 82
|
90
....*....|....*...
gi 1958665283 149 DSLHKFQVKIEKEKVTVR 166
Cdd:COG2146 83 EPLKTYPVRVEDGDVYVD 100
|
|
| Rieske |
cd03467 |
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ... |
71-165 |
7.93e-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: 90.24 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 71 TVCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIGTGDLEDFPGLD 149
Cdd:cd03467 3 VVGALSELPPGGGRVVVVGGGPVVVVrREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSGPAPR 82
|
90
....*....|....*.
gi 1958665283 150 SLHKFQVKIEKEKVTV 165
Cdd:cd03467 83 PLPKYPVKVEGDGVVW 98
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
192-503 |
1.94e-21 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 99.04 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 192 SSTNVLIVGAGAAGLVCAETLRQEGFSDRI---VLCTLDRhLPYDRAKLSKSLDAQ-PEQLALRPKEFFRAYGIEMLTEA 267
Cdd:PRK14989 2 SKVRLAIIGNGMVGHRFIEDLLDKADAANFditVFCEEPR-IAYDRVHLSSYFSHHtAEELSLVREGFYEKHGIKVLVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 268 QVVTVDvRNKKVVFKD-GFKLEYSKLLLAPGSSPKTLTCKGKDIENVFTIRTPEDANRVLRLA-RGRNAVVVGAGFLGME 345
Cdd:PRK14989 81 RAITIN-RQEKVIHSSaGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACArRSKRGAVVGGGLLGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 346 VAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELrAQEGKLQEVVLK--SSKVLRADVCV 423
Cdd:PRK14989 160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEI-VQEGVEARKTMRfaDGSELEVDFIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 424 VGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGDAVtfplAWrNNRKVNI--PHWQMAhaqgRVAAQNMLA 501
Cdd:PRK14989 239 FSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECA----SW-NNRVFGLvaPGYKMA----QVAVDHLLG 309
|
..
gi 1958665283 502 QE 503
Cdd:PRK14989 310 SE 311
|
|
| Rieske |
pfam00355 |
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ... |
72-154 |
7.58e-21 |
|
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: 87.02 E-value: 7.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 72 VCHVKDLENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFNiGTGDLEDFPGLD 149
Cdd:pfam00355 5 VCHSSELPEGEPKVVEVGGEPLVVFRDeDGELYALEDRCPHRGAPLSEGkVNGGGRLECPYHGWRFD-GTGKVVKVPAPR 83
|
....*
gi 1958665283 150 SLHKF 154
Cdd:pfam00355 84 PLKSY 88
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
196-501 |
7.93e-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: 95.20 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFSdrivlCTL-DRHlpyDRA-----------KLSKS-LDAQPEQLalrpkeffRAYGIE 262
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHE-----VTVfEAL---DKPggllrygipefRLPKDvLDREIELI--------EALGVE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 263 MLTEAQV-VTVDVrnkkvvfkDGFKLEYSKLLLAPGSS-PKTLTCKGKDIENVFtirtpeDANRVLR-----------LA 329
Cdd:COG0493 188 FRTNVEVgKDITL--------DELLEEFDAVFLATGAGkPRDLGIPGEDLKGVH------SAMDFLTavnlgeapdtiLA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 330 RGRNAVVVGAGFLGMEVA--AyLTEKAHSVSVVEL---EETPFRRflgERVGRALMkmfENNRVKFYMQTE--------- 395
Cdd:COG0493 254 VGKRVVVIGGGNTAMDCArtA-LRLGAESVTIVYRrtrEEMPASK---EEVEEALE---EGVEFLFLVAPVeiigdengr 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 396 VSELRAQEGKLQE----------VVLKSSKVLRADVCVVGIGAVPATGFLR-QSGIGLDSRGFIPVNKM-MQTNIPGVFA 463
Cdd:COG0493 327 VTGLECVRMELGEpdesgrrrpvPIEGSEFTLPADLVILAIGQTPDPSGLEeELGLELDKRGTIVVDEEtYQTSLPGVFA 406
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958665283 464 AGDAVTFP--LAWrnnrkvniphwqmAHAQGRVAAQNMLA 501
Cdd:COG0493 407 GGDAVRGPslVVW-------------AIAEGRKAARAIDR 433
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
279-511 |
9.18e-19 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 89.45 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 279 VVFKDGFKLEYS--KLLLAPGSSPKtltcKGKDIEnvFTIRTPEDANRVLRLAR-GRNAVVVGAGFLGMEVAAYLTEKAH 355
Cdd:PRK05249 126 VECPDGEVETLTadKIVIATGSRPY----RPPDVD--FDHPRIYDSDSILSLDHlPRSLIIYGAGVIGCEYASIFAALGV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 356 SVSVVELEETPFRrFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLqEVVLKSSKVLRADVCVVGIGAVPATGFL 435
Cdd:PRK05249 200 KVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGV-IVHLKSGKKIKADCLLYANGRTGNTDGL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 436 RQSGIGL--DSRGFIPVNKMMQTNIPGVFAAGDAVTFP-LAwrnnrkvniphwQMAHAQGRVAAQNMLAQEAE--INTVP 510
Cdd:PRK05249 278 NLENAGLeaDSRGQLKVNENYQTAVPHIYAVGDVIGFPsLA------------SASMDQGRIAAQHAVGEATAhlIEDIP 345
|
.
gi 1958665283 511 Y 511
Cdd:PRK05249 346 T 346
|
|
| Rieske_RO_ferredoxin |
cd03528 |
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ... |
72-166 |
4.97e-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: 79.45 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 72 VCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIGTGDLEDFPGLDSL 151
Cdd:cd03528 4 VCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPATEPL 83
|
90
....*....|....*
gi 1958665283 152 HKFQVKIEKEKVTVR 166
Cdd:cd03528 84 KTYPVKVEDGDVYVD 98
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
256-506 |
8.92e-17 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 83.27 E-value: 8.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 256 FRAYGIEMLT-EAQVV---TVDVRNKKV----VFKDgfkleyskLLLAPGSSPKTLtcKGKDIENVfTIRTPEDAnrvLR 327
Cdd:PRK06416 102 LKKNKVDIIRgEAKLVdpnTVRVMTEDGeqtyTAKN--------IILATGSRPREL--PGIEIDGR-VIWTSDEA---LN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 328 LAR-GRNAVVVGAGFLGMEVA-AYLTEKAHsVSVVELEEtpfrRFLG---ERVGRALMKMFENNRVKFYmqTEVSELRAQ 402
Cdd:PRK06416 168 LDEvPKSLVVIGGGYIGVEFAsAYASLGAE-VTIVEALP----RILPgedKEISKLAERALKKRGIKIK--TGAKAKKVE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 403 EGKlQEVVLK-----SSKVLRADVCVVGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTNIPGVFAAGDAVTFP 471
Cdd:PRK06416 241 QTD-DGVTVTledggKEETLEADYVLVAVGRRPNT-----ENLGLEElgvktdRGFIEVDEQLRTNVPNIYAIGDIVGGP 314
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958665283 472 lawrnnrkvniphwQMAH---AQGRVAAQNMLAQEAEI 506
Cdd:PRK06416 315 --------------MLAHkasAEGIIAAEAIAGNPHPI 338
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
196-520 |
4.26e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 80.99 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGfsDRIVLctldrhlpYDRAKL-----------SKSLDAQPEQLALRPKefFRAYGIEml 264
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLG--KKVAL--------IEKGPLggtclnvgcipSKALIAAAEAFHEAKH--AEEFGIH-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 265 teAQVVTVD----------VRNKKVVFKDGFKLEYSKLLLAPGS----SPKTLTCKGKDIE--NVFtI----RTP----- 319
Cdd:PRK06292 72 --ADGPKIDfkkvmarvrrERDRFVGGVVEGLEKKPKIDKIKGTarfvDPNTVEVNGERIEakNIV-IatgsRVPpipgv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 320 --EDANR------VLRLAR-GRNAVVVGAGFLGMEVAAYLtekaHS----VSVVELEEtpfrRFLG---ERVGRALMKMF 383
Cdd:PRK06292 149 wlILGDRlltsddAFELDKlPKSLAVIGGGVIGLELGQAL----SRlgvkVTVFERGD----RILPledPEVSKQAQKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 384 ENnRVKFYMQTEVSELRaQEGKLQEVVLKS---SKVLRADVCVVGIGAVPAT---GfLRQSGIGLDSRGFIPVNKMMQTN 457
Cdd:PRK06292 221 SK-EFKIKLGAKVTSVE-KSGDEKVEELEKggkTETIEADYVLVATGRRPNTdglG-LENTGIELDERGRPVVDEHTQTS 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958665283 458 IPGVFAAGDAVTFPLawrnnrkvniphwqMAHA---QGRVAAQNMLAQEAE-INTVPYLWT-------AMFGKS 520
Cdd:PRK06292 298 VPGIYAAGDVNGKPP--------------LLHEaadEGRIAAENAAGDVAGgVRYHPIPSVvftdpqiASVGLT 357
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
260-521 |
1.05e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 79.97 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 260 GIEMLTEAQVVTV------------DVRNKKVVFKDGFKLEYSKLLLAPGSSPKTLTckgkdienvftiRTPEDANRVL- 326
Cdd:PRK06327 105 GIEGLFKKNKITVlkgrgsfvgktdAGYEIKVTGEDETVITAKHVIIATGSEPRHLP------------GVPFDNKIILd 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 327 ------------RLArgrnavVVGAGFLGMEVAAYLTEKAHSVSVveLEETPfrRFLG---ERVGRALMKMFENNRVKFY 391
Cdd:PRK06327 173 ntgalnftevpkKLA------VIGAGVIGLELGSVWRRLGAEVTI--LEALP--AFLAaadEQVAKEAAKAFTKQGLDIH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 392 MQTEVSELRAQEGKLQ---EVVLKSSKVLRADVCVVGIGAVPATGFLRQSGIGL--DSRGFIPVNKMMQTNIPGVFAAGD 466
Cdd:PRK06327 243 LGVKIGEIKTGGKGVSvayTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLklDERGFIPVDDHCRTNVPNVYAIGD 322
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958665283 467 AVtfplawrnnRKvniphWQMAHA---QGRVAAQNMLAQEAEIN--TVPY-LWT----AMFGKSL 521
Cdd:PRK06327 323 VV---------RG-----PMLAHKaeeEGVAVAERIAGQKGHIDynTIPWvIYTspeiAWVGKTE 373
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
193-466 |
1.49e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 78.81 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 193 STNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRAKLSK--SLDAQPEQLA-LRPKEFFRAYGIEMLTEAQV 269
Cdd:PRK04965 2 SNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHvfSQGQRADDLTrQSAGEFAEQFNLRLFPHTWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 270 VTVDVRNKKVVFKDGfKLEYSKLLLAPGSSPKTLTCKGKdiENVFTIRT-PEDANRVLRLARGRNAVVVGAGFLGMEVAA 348
Cdd:PRK04965 82 TDIDAEAQVVKSQGN-QWQYDKLVLATGASAFVPPIPGR--ELMLTLNSqQEYRAAETQLRDAQRVLVVGGGLIGTELAM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 349 YLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQeVVLKSSKVLRADVCVVGIGA 428
Cdd:PRK04965 159 DLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR-ATLDSGRSIEVDAVIAAAGL 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958665283 429 VPATGFLRQSGIGLDsRGfIPVNKMMQTNIPGVFAAGD 466
Cdd:PRK04965 238 RPNTALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
196-469 |
1.55e-15 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 79.45 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFSdriVlcTL-DRHlpyDRA-----------KLSKSLdaqpeqlALRPKEFFRAYGIEM 263
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYD---V--TIfEAR---DKAggllrygipefRLPKDI-------VDREVERLLKLGVEI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 264 LTEAQV---VTVDvrnkkvvfkdGFKLEYSKLLLAPG-SSPKTLTCKGKDIENVFT----IRTPEDANRVLRLARGRNAV 335
Cdd:PRK11749 208 RTNTEVgrdITLD----------ELRAGYDAVFIGTGaGLPRFLGIPGENLGGVYSavdfLTRVNQAVADYDLPVGKRVV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 336 VVGAGFLGMEVAAylTEK---AHSVSVV---ELEETP---------------FR------RFLGERVGRALMKmfennrv 388
Cdd:PRK11749 278 VIGGGNTAMDAAR--TAKrlgAESVTIVyrrGREEMPaseeevehakeegveFEwlaapvEILGDEGRVTGVE------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 389 kfYMQTEVSELRAQeGKLQEVVLKSSKVLRADVCVVGIGAVPATGFLR-QSGIGLDSRG-FIPVNKMMQTNIPGVFAAGD 466
Cdd:PRK11749 349 --FVRMELGEPDAS-GRRRVPIEGSEFTLPADLVIKAIGQTPNPLILStTPGLELNRWGtIIADDETGRTSLPGVFAGGD 425
|
...
gi 1958665283 467 AVT 469
Cdd:PRK11749 426 IVT 428
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
196-468 |
3.08e-15 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 78.28 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFS----DRivlctldrhlpYDRA-----------KLSKSL-DAQPEQLalrpkeffRAY 259
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKvtvfER-----------ADRIggllrygipdfKLEKEViDRRIELM--------EAE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 260 GIEMLTEAQV-VTVDVrnkkvvfkDGFKLEYSKLLLAPGSS-PKTLTCKGKDIENV-----FTIrtpeDANRVLR----- 327
Cdd:PRK12810 207 GIEFRTNVEVgKDITA--------EELLAEYDAVFLGTGAYkPRDLGIPGRDLDGVhfamdFLI----QNTRRVLgdete 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 328 ---LARGRNAVVVGAGFLGME-VAAYLTEKAhsVSVVELEET---PFRRFLGERVGRALMKMfennRVK----------F 390
Cdd:PRK12810 275 pfiSAKGKHVVVIGGGDTGMDcVGTAIRQGA--KSVTQRDIMpmpPSRRNKNNPWPYWPMKL----EVSnaheegvereF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 391 YMQTE--------VSELRAQEGKLQ----EVVLKSSKVLRADVCVVGIGAVPA-TGFLRQSGIGLDSRGFIPVNKM-MQT 456
Cdd:PRK12810 349 NVQTKefegengkVTGVKVVRTELGegdfEPVEGSEFVLPADLVLLAMGFTGPeAGLLAQFGVELDERGRVAAPDNaYQT 428
|
330
....*....|..
gi 1958665283 457 NIPGVFAAGDAV 468
Cdd:PRK12810 429 SNPKVFAAGDMR 440
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
244-499 |
3.46e-13 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 71.72 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 244 QPeQLALRPKEFFRAYGIEMLTEAQVVTVDVRNKKV-VFKDGFKLEYSKLLLAPGSSPKTLTCKG--------KDIENVF 314
Cdd:PTZ00318 69 RP-ALAKLPNRYLRAVVYDVDFEEKRVKCGVVSKSNnANVNTFSVPYDKLVVAHGARPNTFNIPGveerafflKEVNHAR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 315 TIR---------------TPEDANRVLRLargrnaVVVGAGFLGMEVAAYLTE--------------KAHSVSVVELEET 365
Cdd:PTZ00318 148 GIRkrivqcieraslpttSVEERKRLLHF------VVVGGGPTGVEFAAELADffrddvrnlnpelvEECKVTVLEAGSE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 366 PFRRFlGERVGRALMKMFENNRVKFYMQTEVSELraqegKLQEVVLKSSKVLRADVCV--VGIGAVPATgflRQSGIGLD 443
Cdd:PTZ00318 222 VLGSF-DQALRKYGQRRLRRLGVDIRTKTAVKEV-----LDKEVVLKDGEVIPTGLVVwsTGVGPGPLT---KQLKVDKT 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958665283 444 SRGFIPVNKMMQT-NIPGVFAAGDAVTfplawrNNRKVNIPHWQMAHAQGRVAAQNM 499
Cdd:PTZ00318 293 SRGRISVDDHLRVkPIPNVFALGDCAA------NEERPLPTLAQVASQQGVYLAKEF 343
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
248-467 |
1.96e-12 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 69.84 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 248 LALRPKEFFRAYGI--EMLTEAQVV-------TVDVRNKKVVFKDGFKLEYS--KLLLAPGSSPKTLTCKGKDIEnvfti 316
Cdd:PLN02507 116 LQKKTDEILRLNGIykRLLANAGVKlyegegkIVGPNEVEVTQLDGTKLRYTakHILIATGSRAQRPNIPGKELA----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 317 RTPEDANRVLRLARgrNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERvgRALM-KMFENNRVKFYMQTE 395
Cdd:PLN02507 191 ITSDEALSLEELPK--RAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEM--RAVVaRNLEGRGINLHPRTN 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958665283 396 VSELRAQEGKLQeVVLKSSKVLRADVCVVGIGAVPATGF--LRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGDA 467
Cdd:PLN02507 267 LTQLTKTEGGIK-VITDHGEEFVADVVLFATGRAPNTKRlnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
196-471 |
5.50e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 67.32 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpYDRaklsksldaQPEQLAL--------R-PKEFFRAyGIEMLTE 266
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGYEVHV----------YDK---------LPEPGGLmlfgipefRiPIERVRE-GVKELEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 267 AQVVTVDvrNKKVVF-------------KDGFKLE-----YSKLLLAPGS-SPKTLTCKGKDIENV-------FTIRTPE 320
Cdd:PRK12770 81 AGVVFHT--RTKVCCgeplheeegdefvERIVSLEelvkkYDAVLIATGTwKSRKLGIPGEDLPGVysaleylFRIRAAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 321 ----DANRVLRLArGRNAVVVGAGFLGMEVA--AYLtEKAHSVSVV---ELEETPFRRFLGERVGRALMKMFEN-NRVKF 390
Cdd:PRK12770 159 lgylPWEKVPPVE-GKKVVVVGAGLTAVDAAleAVL-LGAEKVYLAyrrTINEAPAGKYEIERLIARGVEFLELvTPVRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 391 YMQTEVSELRAQEGKLQ----------EVVLKSSKVLRADVCVVGIGAVPATGFLRQS-GIGLDSRGFIPVNKMMQTNIP 459
Cdd:PRK12770 237 IGEGRVEGVELAKMRLGepdesgrprpVPIPGSEFVLEADTVVFAIGEIPTPPFAKEClGIELNRKGEIVVDEKHMTSRE 316
|
330
....*....|..
gi 1958665283 460 GVFAAGDAVTFP 471
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 |
1.31e-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: 61.84 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKG-VLSRGRVRCPWHGACFN-----IGTGDLE 143
Cdd:cd03469 4 VGHSSELpEPGDYVTLELGGEPLVLVRDrDGEVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYDldgklVGVPREE 83
|
90
....*....|....*....
gi 1958665283 144 DFPGLD----SLHKFQVKI 158
Cdd:cd03469 84 GFPGFDkeklGLRTVPVEE 102
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
195-517 |
1.85e-11 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 66.38 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 195 NVLIVGAGAAGLVCAETLRQEGFsdRIVLctLDRHL-----------PydraklSKSL--DAQPEQLALRPKEffraYGI 261
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGM--KVAL--IERGLlggtcvntgcvP------TKTLiaSARAAHLARRAAE----YGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 262 emlTEAQVVTVDVrnKKVV-FKDGFKleysklllapGSSPKTLTCKGKDIENVFTIR---TPEDANRVL---RLARGRNA 334
Cdd:PRK06370 73 ---SVGGPVSVDF--KAVMaRKRRIR----------ARSRHGSEQWLRGLEGVDVFRghaRFESPNTVRvggETLRAKRI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 335 VV-VGA-----GFLGMEVAAYLTekahSVSVVELEETP------------------FRRF--------LGER-------- 374
Cdd:PRK06370 138 FInTGAraaipPIPGLDEVGYLT----NETIFSLDELPehlviigggyiglefaqmFRRFgsevtvieRGPRllpreded 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 375 VGRALMKMFENNRVKFYMQTEVSEL-RAQEGKLQEVVLKS-SKVLRADVCVVGIGAVPATGF--LRQSGIGLDSRGFIPV 450
Cdd:PRK06370 214 VAAAVREILEREGIDVRLNAECIRVeRDGDGIAVGLDCNGgAPEITGSHILVAVGRVPNTDDlgLEAAGVETDARGYIKV 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958665283 451 NKMMQTNIPGVFAAGDavtfplawrnnrkVNIPhWQMAH---AQGRVAAQNML---AQEAEINTVPYlwtAMF 517
Cdd:PRK06370 294 DDQLRTTNPGIYAAGD-------------CNGR-GAFTHtayNDARIVAANLLdggRRKVSDRIVPY---ATY 349
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
335-466 |
1.92e-11 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 66.33 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 335 VVVGAGFLGMEVAAYLtekaHSVSV-VEL---EETPFRRFLGErVGRALMKMFENNRVKFYMQTEVSELRAQ-EGKLQeV 409
Cdd:PRK06116 171 AVVGAGYIAVEFAGVL----NGLGSeTHLfvrGDAPLRGFDPD-IRETLVEEMEKKGIRLHTNAVPKAVEKNaDGSLT-L 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958665283 410 VLKSSKVLRADVCVVGIGAVPAT-GF-LRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGD 466
Cdd:PRK06116 245 TLEDGETLTVDCLIWAIGREPNTdGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGD 303
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
333-413 |
1.97e-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: 59.91 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 333 NAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPfRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKlQEVVLK 412
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL-LPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDG-VVVVLT 78
|
.
gi 1958665283 413 S 413
Cdd:pfam00070 79 D 79
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
254-466 |
2.69e-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: 66.15 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 254 EFFRAYGieMLTEAQVVTV-DVRNKKVVFKDGFKLEYskLLLAPGSSPKTLTCKGKD--IENVFTIRTPEDANRVLrlar 330
Cdd:TIGR01423 120 TFFLGWG--ALEDKNVVLVrESADPKSAVKERLQAEH--ILLATGSWPQMLGIPGIEhcISSNEAFYLDEPPRRVL---- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 331 grnavVVGAGFLGMEVAAYLTEKAHSVSVVEL--EETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQE 408
Cdd:TIGR01423 192 -----TVGGGFISVEFAGIFNAYKPRGGKVTLcyRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKH 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 409 VVLKSSKVLRADVCVVGIGAVPATGFLR--QSGIGLDSRGFIPVNKMMQTNIPGVFAAGD 466
Cdd:TIGR01423 267 VTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
273-516 |
6.26e-11 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 65.17 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 273 DVRNKKVVFKDGFKLE--YSKLLLAPGSSPKTLTCKG-KD------IENVFTIRTPEdanrvlRLArgrnavVVGAGFLG 343
Cdd:PRK13748 215 DDQTLIVRLNDGGERVvaFDRCLIATGASPAVPPIPGlKEtpywtsTEALVSDTIPE------RLA------VIGSSVVA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 344 MEVAAYLTEKAHSVSVVELEETPFRRflGERVGRALMKMFENNRVKFYMQTEVSELRAQEGklqEVVLKSSK-VLRADVC 422
Cdd:PRK13748 283 LELAQAFARLGSKVTILARSTLFFRE--DPAIGEAVTAAFRAEGIEVLEHTQASQVAHVDG---EFVLTTGHgELRADKL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 423 VVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNIPGVFAAGDAVTFPlawrnnrkvniphwQ---MAHAQGRVAAQ 497
Cdd:PRK13748 358 LVATGRAPNTRSLalDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP--------------QfvyVAAAAGTRAAI 423
|
250
....*....|....*....
gi 1958665283 498 NMLAQEAEINTvpylwTAM 516
Cdd:PRK13748 424 NMTGGDAALDL-----TAM 437
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
283-468 |
8.00e-10 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 61.55 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 283 DGFKLEYSKLLLAPGSSPKTLTCKGKDienvFTIrtpeDANRVLRLARGRNAVVVGAGFLGMEVAAYLTEKAHSVSVVEL 362
Cdd:PTZ00058 197 DGQVIEGKNILIAVGNKPIFPDVKGKE----FTI----SSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 363 EETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSEL-RAQEGKLQEVVLKSSKVLRADVCVVGIGAVPATGFLRQSGIG 441
Cdd:PTZ00058 269 GNRLLRKF-DETIINELENDMKKNNINIITHANVEEIeKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALN 347
|
170 180
....*....|....*....|....*...
gi 1958665283 442 -LDSRGFIPVNKMMQTNIPGVFAAGDAV 468
Cdd:PTZ00058 348 iKTPKGYIKVDDNQRTSVKHIYAVGDCC 375
|
|
| Rieske_NirD_small_Bacillus |
cd03530 |
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ... |
71-163 |
1.20e-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: 55.69 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 71 TVCHVKDLENGQMREVELGWGKVLLVK-DNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIGTGDLEDfPGLD 149
Cdd:cd03530 3 DIGALEDIPPRGARKVQTGGGEIAVFRtADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQG-PDEG 81
|
90
....*....|....
gi 1958665283 150 SLHKFQVKIEKEKV 163
Cdd:cd03530 82 CVRTFPVKVEDGRV 95
|
|
| Rieske_T4moC |
cd03474 |
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ... |
72-166 |
9.39e-09 |
|
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.
Pssm-ID: 239556 [Multi-domain] Cd Length: 108 Bit Score: 53.50 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 72 VCHVKDLENGQMREVELGWGKVLLV-KDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIGTGDLEDfPGLDS 150
Cdd:cd03474 4 VCSLDDVWEGEMELVDVDGEEVLLVaPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGLN-PRDCR 82
|
90
....*....|....*.
gi 1958665283 151 LHKFQVKIEKEKVTVR 166
Cdd:cd03474 83 LARYPVKVEGGDILVD 98
|
|
| Reductase_C |
pfam14759 |
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ... |
511-561 |
1.83e-08 |
|
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerization. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).
Pssm-ID: 434185 [Multi-domain] Cd Length: 83 Bit Score: 51.80 E-value: 1.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958665283 511 YLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMN 561
Cdd:pfam14759 1 WFWSDQYDLKLQIAGLPTGADEVVLRGDPEDGAFSVFYLRDGRLVAVDAVN 51
|
|
| HcaE |
COG4638 |
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ... |
72-156 |
1.86e-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: 56.15 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 72 VCHVKDL-ENGQMREVELGWGKVLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFN-----IGTGDLED 144
Cdd:COG4638 30 VGHSSELpEPGDYLTRTILGEPVVLVRDkDGEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDldgrlVGIPHMEG 109
|
90
....*....|....*.
gi 1958665283 145 FPGLD----SLHKFQV 156
Cdd:COG4638 110 FPDFDparaGLRSVPV 125
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
293-495 |
2.41e-08 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 56.79 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 293 LLAPGSSPKTLTCKGKDIENVFTIRT-------PEdanrvlRLargrnaVVVGAGFLGMEVAAYLTEKAHSVSVV----- 360
Cdd:PRK07845 144 LIATGASPRILPTAEPDGERILTWRQlydldelPE------HL------IVVGSGVTGAEFASAYTELGVKVTLVssrdr 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 361 ----------ELEETPFRRflgervgRAlMKMFENNRVKfymqtevSELRAQEGklQEVVLKSSKVLRADVCVVGIGAVP 430
Cdd:PRK07845 212 vlpgedadaaEVLEEVFAR-------RG-MTVLKRSRAE-------SVERTGDG--VVVTLTDGRTVEGSHALMAVGSVP 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 431 AT---GfLRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGDaVT--FPLAwrnnrkvniphwQMAHAQGRVA 495
Cdd:PRK07845 275 NTaglG-LEEAGVELTPSGHITVDRVSRTSVPGIYAAGD-CTgvLPLA------------SVAAMQGRIA 330
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
185-496 |
3.02e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 56.66 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 185 ISPSAGHSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctldrhlpydraklsksLDAQPEqlalrPKEFFRaYGI--- 261
Cdd:PRK12814 185 IPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTI-------------------FDANEQ-----AGGMMR-YGIprf 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 262 ---EMLTEAQV-----VTVDVRNKKVVFKD----GFKLEYSKLLLAPGSS-PKTLTCKGKDIENVFT-IRTPEDANRVLR 327
Cdd:PRK12814 240 rlpESVIDADIaplraMGAEFRFNTVFGRDitleELQKEFDAVLLAVGAQkASKMGIPGEELPGVISgIDFLRNVALGTA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 328 LARGRNAVVVGAGFLGMEVA-AYLTEKAHSVSVV---ELEETPFRRflgERVGRALMkmfENNRVKFYM----------Q 393
Cdd:PRK12814 320 LHPGKKVVVIGGGNTAIDAArTALRLGAESVTILyrrTREEMPANR---AEIEEALA---EGVSLRELAapvsiersegG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 394 TEVSELRAQEGKLQE------VVLKSSK-VLRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNIPGVFAAG 465
Cdd:PRK12814 394 LELTAIKMQQGEPDEsgrrrpVPVEGSEfTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPeTLQTSVAGVFAGG 473
|
330 340 350
....*....|....*....|....*....|..
gi 1958665283 466 DAVTFP-LAWRnnrkvniphwqmAHAQGRVAA 496
Cdd:PRK12814 474 DCVTGAdIAIN------------AVEQGKRAA 493
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
336-466 |
3.55e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 55.91 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 336 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFlgERVGRALMKMF-ENNRVKFYMQTEVSELRAQEGKLqeVVLKSS 414
Cdd:PRK07251 162 IIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE--EPSVAALAKQYmEEDGITFLLNAHTTEVKNDGDQV--LVVTED 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958665283 415 KVLRADVCVVGIGAVPATG--FLRQSGIGLDSRGFIPVNKMMQTNIPGVFAAGD 466
Cdd:PRK07251 238 ETYRFDALLYATGRKPNTEplGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
317-500 |
4.92e-08 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 55.73 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 317 RTPEDanrVLRLAR-GRNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRF---LGERVGRALMKmfennRVKFYM 392
Cdd:PRK07846 154 HTSDT---IMRLPElPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLdddISERFTELASK-----RWDVRL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 393 QTEVSELRAQEGKLqEVVLKSSKVLRADVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNIPGVFAAGDaVTF 470
Cdd:PRK07846 226 GRNVVGVSQDGSGV-TLRLDDGSTVEADVLLVATGRVPNGDLLdaAAAGVDVDEDGRVVVDEYQRTSAEGVFALGD-VSS 303
|
170 180 190
....*....|....*....|....*....|...
gi 1958665283 471 PlawrnnrkvniphWQMAH---AQGRVAAQNML 500
Cdd:PRK07846 304 P-------------YQLKHvanHEARVVQHNLL 323
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
227-517 |
7.44e-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: 55.24 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 227 DRHLPYDRAKLSKSLDAQPEQL------ALRPKE--FFRAYGieMLTEAQVVTVDVRNKKVVFKDGfkleySKLLLAPGS 298
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLnwgyrvALREKKvkYENAYA--EFVDKHRIKATNKKGKEKIYSA-----ERFLIATGE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 299 SPKTLTCKG-KDI----ENVFTIrtPEDANRVLrlargrnavVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFlGE 373
Cdd:TIGR01438 154 RPRYPGIPGaKELcitsDDLFSL--PYCPGKTL---------VVGASYVALECAGFLAGIGLDVTVM-VRSILLRGF-DQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 374 RVGRALMKMFENNRVKFYMQTEVSELRAQEGKlqeVVLKSSKVLRA-----DVCVVGIGAVPATgflrqSGIGLDSRGF- 447
Cdd:TIGR01438 221 DCANKVGEHMEEHGVKFKRQFVPIKVEQIEAK---VLVEFTDSTNGieeeyDTVLLAIGRDACT-----RKLNLENVGVk 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958665283 448 -------IPVNKMMQTNIPGVFAAGDAVtfplawrNNRKVNIPhwqMAHAQGRVAAQNMLAQEAEINTVPYLWTAMF 517
Cdd:TIGR01438 293 inkktgkIPADEEEQTNVPYIYAVGDIL-------EDKPELTP---VAIQAGRLLAQRLFKGSTVICDYENVPTTVF 359
|
|
| PobA |
COG5749 |
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]; |
72-149 |
2.16e-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: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 72 VCHVKDLENGQMREVELgWGK-VLLVKD-NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiGTGDLEDFPGLD 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 ... |
100-147 |
2.69e-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: 2.69e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958665283 100 GEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiGTGDLEDFPG 147
Cdd:cd03532 37 GRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFD-SDGRCVHMPG 83
|
|
| PRK09965 |
PRK09965 |
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional |
72-165 |
3.19e-07 |
|
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
Pssm-ID: 170182 [Multi-domain] Cd Length: 106 Bit Score: 49.00 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 72 VCHVKDLENGQMREVELGwGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLS-RGRVRCPWHGACFNIGTGDLEDFPGLDS 150
Cdd:PRK09965 6 ACPVADLPEGEALRVDTS-PVIALFNVGGEFYAIDDRCSHGNASLSEGYLEdDATVECPLHAASFCLRTGKALCLPATDP 84
|
90
....*....|....*
gi 1958665283 151 LHKFQVKIEKEKVTV 165
Cdd:PRK09965 85 LRTYPVHVEGGDIFI 99
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
424-471 |
4.83e-07 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 52.47 E-value: 4.83e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958665283 424 VGIGAVPATGFLRQSgIGLDSRGFIPVNKMMQTNIPGVFAAGDAVTFP 471
Cdd:PRK15317 443 VQIGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVP 489
|
|
| QcrA/PetC |
COG0723 |
Rieske Fe-S protein [Energy production and conversion]; |
75-165 |
6.94e-07 |
|
Rieske Fe-S protein [Energy production and conversion];
Pssm-ID: 440487 [Multi-domain] Cd Length: 118 Bit Score: 48.46 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 75 VKDLENGQMREVELGWGKVLLVK----DNGEFHALGHKCPHYGAPlVKGVLSRGRVRCPWHGACFNIG----TGdledfP 146
Cdd:COG0723 23 LSDLPPGEGKVVEWRGKPVFVVRtpvrGDGEIVAVSAICTHLGCP-VTWNADEGGFDCPCHGSRFDPDgrvlKG-----P 96
|
90
....*....|....*....
gi 1958665283 147 GLDSLHKFQVKIEKEKVTV 165
Cdd:COG0723 97 APRPLPVPPLEVDDDKLLI 115
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
282-467 |
1.45e-06 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 51.45 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 282 KDGFKLEYSKLLLAPGSSPKTLTCKGKDIENVFTirtpedANRVLRLARGRNAV-VVGAGFLGMEVAAYLTekAHSVSVV 360
Cdd:PTZ00153 268 KSGKEFKVKNIIIATGSTPNIPDNIEVDQKSVFT------SDTAVKLEGLQNYMgIVGMGIIGLEFMDIYT--ALGSEVV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 361 ELEETP-FRRFLGERVGRALMKMFENNR-VKFYMQTEVSELRAQEGKlQEVVLKSS-----------------KVLRADV 421
Cdd:PTZ00153 340 SFEYSPqLLPLLDADVAKYFERVFLKSKpVRVHLNTLIEYVRAGKGN-QPVIIGHSerqtgesdgpkknmndiKETYVDS 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958665283 422 CVVGIGAVPATgflrqSGIGLDS------RGFIPVNKMMQTN------IPGVFAAGDA 467
Cdd:PTZ00153 419 CLVATGRKPNT-----NNLGLDKlkiqmkRGFVSVDEHLRVLredqevYDNIFCIGDA 471
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
196-471 |
2.53e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 50.54 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFsDRIVLCTLDR------------HLPYDraklskSLDaqpeqlalRPKEFFRAYGIEM 263
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKpggvmrygipsyRLPDE------ALD--------KDIAFIEALGVKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 264 LTEAQVVtvdvrnKKVVFKDgFKLEYSKLLLAPG-SSPKTLTCKGKDIENVFtirtpeDANRVLRLARG----------- 331
Cdd:PRK13984 351 HLNTRVG------KDIPLEE-LREKHDAVFLSTGfTLGRSTRIPGTDHPDVI------QALPLLREIRDylrgegpkpki 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 332 -RNAVVVGAGFLGMEVAAYLTE------KAHSVSVVELEET---------PFRRFLGERV----GRALMK-MFENNRVKF 390
Cdd:PRK13984 418 pRSLVVIGGGNVAMDIARSMARlqkmeyGEVNVKVTSLERTfeempadmeEIEEGLEEGVviypGWGPMEvVIENDKVKG 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 391 YMQTEVSELRAQEGKLQEVVLKSSK-VLRADVCVVGIGAVPATGFLRQSgigLDS-----RGFIPVNKMMQTNIPGVFAA 464
Cdd:PRK13984 498 VKFKKCVEVFDEEGRFNPKFDESDQiIVEADMVVEAIGQAPDYSYLPEE---LKSklefvRGRILTNEYGQTSIPWLFAG 574
|
....*..
gi 1958665283 465 GDAVTFP 471
Cdd:PRK13984 575 GDIVHGP 581
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
196-499 |
4.19e-06 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 49.87 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFSdrivlCTLdrhlpydraklsksLDAQPeQLA--LRpkeffraYGI-------EML-T 265
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHA-----VTI--------------FEAGP-KLGgmMR-------YGIpayrlprEVLdA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 266 EAQVVT---VDVRNKKVVFKD--GFKLE--YSKLLLAPG-SSPKTLTCKGKDIENVFT----IRTPEDANRVLRlarGRN 333
Cdd:PRK12771 193 EIQRILdlgVEVRLGVRVGEDitLEQLEgeFDAVFVAIGaQLGKRLPIPGEDAAGVLDavdfLRAVGEGEPPFL---GKR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 334 AVVVGAGFLGMEVAAylTEK---AHSVSVV-------------ELEE------------TPfRRFLGERVGRALMKMfen 385
Cdd:PRK12771 270 VVVIGGGNTAMDAAR--TARrlgAEEVTIVyrrtredmpahdeEIEEalregveinwlrTP-VEIEGDENGATGLRV--- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 386 nrVKFYMQTEVSELRAQEGKLQEVVLKsskvlrADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKM-MQTNIPGVFAA 464
Cdd:PRK12771 344 --ITVEKMELDEDGRPSPVTGEEETLE------ADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPNfMMTGRPGVFAG 415
|
330 340 350
....*....|....*....|....*....|....*
gi 1958665283 465 GDAVTFPlawrnnRKVNiphwqMAHAQGRVAAQNM 499
Cdd:PRK12771 416 GDMVPGP------RTVT-----TAIGHGKKAARNI 439
|
|
| Rieske_RO_Alpha_OMO_CARDO |
cd03548 |
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ... |
76-144 |
8.35e-06 |
|
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: 45.88 E-value: 8.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958665283 76 KDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGV--LSRGRVRCPWHGACFNIGTGDLED 144
Cdd:cd03548 22 HELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPecFTKGTITCWYHGWTYRLDDGKLVT 92
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
196-469 |
1.02e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 48.48 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFSDRI--VLCTLDRHLPYdraklsksldAQPEqlaLR-PKEFFRAYGIEMLTEAQV--V 270
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIfeALHEPGGVLVY----------GIPE---FRlPKETVVKKEIENIKKLGVkiE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 271 TVDVRNKKVVFKDGFKLE-YSKLLLAPGSS-PKTLTCKGKDIENVFTirtpedANRVLR---------------LARGRN 333
Cdd:PRK12831 210 TNVVVGKTVTIDELLEEEgFDAVFIGSGAGlPKFMGIPGENLNGVFS------ANEFLTrvnlmkaykpeydtpIKVGKK 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 334 AVVVGAGFLGMEVAAY---LTEKAHSVSVVELEETPFRRflgERVGRAL-----MKMF---------ENNRVKfYMQTEV 396
Cdd:PRK12831 284 VAVVGGGNVAMDAARTalrLGAEVHIVYRRSEEELPARV---EEVHHAKeegviFDLLtnpveilgdENGWVK-GMKCIK 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958665283 397 SEL--RAQEGKLQEVVLKSSK-VLRADVCVVGIGAVPATGFLRQS-GIGLDSRGFIPVNK-MMQTNIPGVFAAGDAVT 469
Cdd:PRK12831 360 MELgePDASGRRRPVEIEGSEfVLEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADEeTGLTSKEGVFAGGDAVT 437
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
336-466 |
2.53e-05 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 46.93 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 336 VVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRfLGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQevVLKSSK 415
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHENQVQ--VHSEHA 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958665283 416 VLRADVCVVGIGAVPATGFL--RQSGIGLDSRGFIPVNKMMQTNIPGVFAAGD 466
Cdd:PRK08010 240 QLAVDALLIASGRQPATASLhpENAGIAVNERGAIVVDKYLHTTADNIWAMGD 292
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
330-465 |
5.21e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 45.68 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 330 RGRNAVVVGAGFLGMEVAAYLTEKAHSVSVV------ELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRAQE 403
Cdd:pfam13738 154 AGQKVVVIGGYNSAVDAALELVRKGARVTVLyrgsewEDRDSDPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKEITEVD 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958665283 404 GklqEVVLKSS---KVLRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNK-MMQTNIPGVFAAG 465
Cdd:pfam13738 234 V---SYKVHTEdgrKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEeTESTNVPGLFLAG 296
|
|
| Rieske_RO_Alpha_PaO |
cd03480 |
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ... |
56-146 |
6.22e-05 |
|
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: 43.08 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 56 PTPQPYPSPQDCVEA--TVCHVKDLENGQMRevelgwGKVLLVKD--------NGEFHALGHKCPHYGAPLVKGVLSR-G 124
Cdd:cd03480 3 PAGGSDSDKFDWREVwyPVAYVEDLDPSRPT------PFTLLGRDlviwwdrnSQQWRAFDDQCPHRLAPLSEGRIDEeG 76
|
90 100
....*....|....*....|..
gi 1958665283 125 RVRCPWHGACFNiGTGDLEDFP 146
Cdd:cd03480 77 CLECPYHGWSFD-GSGSCQRIP 97
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
331-469 |
9.48e-05 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 45.50 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 331 GRNAVVVGAGFLGMEVAAylTEK---AHSVSVV---ELEETPFRRflgERVGRALMK----MFENNRVKfYMQTE---VS 397
Cdd:PRK12778 570 GKKVAVVGGGNTAMDSAR--TAKrlgAERVTIVyrrSEEEMPARL---EEVKHAKEEgiefLTLHNPIE-YLADEkgwVK 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 398 ELRAQEGKLQE---------VVLKSSKV-LRADVCVVGIGAVPATGFLRQ-SGIGLDSRGFIPVNKMMQTNIPGVFAAGD 466
Cdd:PRK12778 644 QVVLQKMELGEpdasgrrrpVAIPGSTFtVDVDLVIVSVGVSPNPLVPSSiPGLELNRKGTIVVDEEMQSSIPGIYAGGD 723
|
...
gi 1958665283 467 AVT 469
Cdd:PRK12778 724 IVR 726
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
196-500 |
2.19e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 44.35 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFSDRIvlctLDRH----------LPydRAKLSKSLDAqpeqlalRPKEFFRAYGIEMLT 265
Cdd:PRK12769 330 VAIIGAGPAGLACADVLARNGVAVTV----YDRHpeigglltfgIP--AFKLDKSLLA-------RRREIFSAMGIEFEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 266 EAQVvtvdvrnKKVVFKDGFKLEYSKLLLAPGsspkTLTCKGKDIENvftirtpEDA--------------NRVLRLA-- 329
Cdd:PRK12769 397 NCEV-------GKDISLESLLEDYDAVFVGVG----TYRSMKAGLPN-------EDApgvydalpfliantKQVMGLEel 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 330 --------RGRNAVVVGAGFLGME-VAAYLTEKAHSV-------------SVVEL----EETPFRRFLGERVGRALMKMF 383
Cdd:PRK12769 459 peepfintAGLNVVVLGGGDTAMDcVRTALRHGASNVtcayrrdeanmpgSKKEVknarEEGANFEFNVQPVALELNEQG 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 384 ENNRVKFyMQTEVSELRAQeGKLQEVVLKSSK-VLRADVCVVGIGAVPAT-GFLRQSGIGLDSRGFI--PVNKMM--QTN 457
Cdd:PRK12769 539 HVCGIRF-LRTRLGEPDAQ-GRRRPVPIPGSEfVMPADAVIMAFGFNPHGmPWLESHGVTVDKWGRIiaDVESQYryQTS 616
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958665283 458 IPGVFAAGDAVtfplawRNNRKVniphwQMAHAQGRVAAQNML 500
Cdd:PRK12769 617 NPKIFAGGDAV------RGADLV-----VTAMAEGRHAAQGII 648
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
195-284 |
3.31e-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: 39.49 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 195 NVLIVGAGAAGLVCAETLRQEGfSDRIVLCTLDRHLPYDRAKLSKSLdaqpeqlalrpKEFFRAYGIEMLTEAQV--VTV 272
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLG-SKVTVVERRDRLLPGFDPEIAKIL-----------QEKLEKNGIEFLLNTTVeaIEG 68
|
90
....*....|..
gi 1958665283 273 DVRNKKVVFKDG 284
Cdd:pfam00070 69 NGDGVVVVLTDG 80
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
192-218 |
5.06e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 42.56 E-value: 5.06e-04
10 20
....*....|....*....|....*..
gi 1958665283 192 SSTNVLIVGAGAAGLVCAETLRQEGFS 218
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHE 28
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
198-229 |
5.07e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 38.67 E-value: 5.07e-04
10 20 30
....*....|....*....|....*....|..
gi 1958665283 198 IVGAGAAGLVCAETLRQEGFsdRIVLctLDRH 229
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGF--RVLV--LEKR 28
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
196-221 |
5.61e-04 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 42.60 E-value: 5.61e-04
10 20 30
....*....|....*....|....*....|...
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGF-------SDRI 221
Cdd:COG1231 10 VVIVGAGLAGLAAARELRKAGLdvtvleaRDRV 42
|
|
| Rieske_RO_Alpha_Cao |
cd04337 |
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ... |
76-146 |
5.70e-04 |
|
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: 40.17 E-value: 5.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958665283 76 KDLENGQMREVEL---GWgkVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNiGTGDLEDFP 146
Cdd:cd04337 25 KDLKMDTMVPFELfgqPW--VLFRDEDGTPGCIRDECAHRACPLSLGKVIEGRIQCPYHGWEYD-GDGECTKMP 95
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
335-517 |
9.12e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 42.12 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 335 VVVGAGFLGMEVAAYLTEKAHSVSVVeLEETPFRRFlGERVGRALMKMFENNRVKFYMQTEVSELRAQEGKLQeVVLKSS 414
Cdd:PTZ00052 186 LIVGASYIGLETAGFLNELGFDVTVA-VRSIPLRGF-DRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIK-VLFSDG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 415 KVLRADVCVVGIGAVPATGFLRQSGIGL---DSRGFIPVNKMmqTNIPGVFAAGDAVtfplawrnnrkVNIPHWQ-MAHA 490
Cdd:PTZ00052 263 TTELFDTVLYATGRKPDIKGLNLNAIGVhvnKSNKIIAPNDC--TNIPNIFAVGDVV-----------EGRPELTpVAIK 329
|
170 180
....*....|....*....|....*..
gi 1958665283 491 QGRVAAQNMLAQEAEINTVPYLWTAMF 517
Cdd:PTZ00052 330 AGILLARRLFKQSNEFIDYTFIPTTIF 356
|
|
| Rieske_RO_Alpha_PhDO_like |
cd03479 |
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ... |
99-158 |
2.39e-03 |
|
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of PhDO and similar proteins including 3-chlorobenzoate 3,4-dioxygenase (CBDO), phenoxybenzoate dioxygenase (POB-dioxygenase) and 3-nitrobenzoate oxygenase (MnbA). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PhDO and CBDO are two-component RO systems, containing oxygenase and reductase components. PhDO catalyzes the dihydroxylation of phthalate to form the 4,5-dihydro-cis-dihydrodiol of phthalate (DHD). CBDO, together with CbaC dehydrogenase, converts the environmental pollutant 3CBA to protocatechuate (PCA) and 5-Cl-PCA, which are then metabolized by the chromosomal PCA meta (extradiol) ring fission pathway. POB-dioxygenase catalyzes the initial catabolic step in the angular dioxygenation of phenoxybenzoate, converting mono- and dichlorinated phenoxybenzoates to protocatechuate and chlorophenols. These phenoxybenzoates are metabolic products formed during the degradation of pyrethroid insecticides.
Pssm-ID: 239561 [Multi-domain] Cd Length: 144 Bit Score: 38.77 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958665283 99 NGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNIgTGDLEDFPGL--DSLHKFQVKI 158
Cdd:cd03479 54 SGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFDV-DGQCLEMPSEppDSQLKQKVRQ 114
|
|
| SfcA |
COG0281 |
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ... |
196-229 |
4.69e-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: 39.61 E-value: 4.69e-03
10 20 30
....*....|....*....|....*....|....*
gi 1958665283 196 VLIVGAGAAGLVCAETLRQEGFS-DRIVLCtlDRH 229
Cdd:COG0281 194 IVINGAGAAGIAIARLLVAAGLSeENIIMV--DSK 226
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
197-218 |
5.72e-03 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 39.26 E-value: 5.72e-03
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
330-468 |
8.80e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 38.50 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665283 330 RGRNAVVVGAGFLGMEVAAYLTEKAHSVSVVELEETpfrrFLGERVG-RALMKMFENNRVKFYMQTEVSELRAQEGKLQE 408
Cdd:PRK10262 145 RNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG----FRAEKILiKRLMDKVENGNIILHTNRTLEEVTGDQMGVTG 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958665283 409 VVLKSSK------VLRADVCVVGIGAVPATGFLrQSGIGLDSrGFIPVNKMM-----QTNIPGVFAAGDAV 468
Cdd:PRK10262 221 VRLRDTQnsdnieSLDVAGLFVAIGHSPNTAIF-EGQLELEN-GYIKVQSGIhgnatQTSIPGVFAAGDVM 289
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
188-229 |
9.47e-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: 9.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958665283 188 SAGHSSTNVLIVGAGAAGLVCAETLRQEGFSDRIvlctLDRH 229
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVV----LEKA 38
|
|
| |
