|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
4-394 |
3.00e-134 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 390.27 E-value: 3.00e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 4 QRAVIIGASHAGAQLATSLRQERWTGEIVLIGDESALPYQRPPLSKaYLASKSTLKDLEIRSVEFYSKHGIQLR-DATVE 82
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSK-VLAGETDEEDLLLRPADFYEENGIDLRlGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 83 AIDRSAGSLSLSTGDALTYDKLALCTGARPRRLPTPGADLAGVYYLRTAADVGLIRKAANPGRRAVIVGGGYIGLETAAS 162
Cdd:COG1251 81 AIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 163 LRALGLEVTVLEATERVLERVTAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLASGESIPADLLIIGIGVEP 242
Cdd:COG1251 161 LRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 243 NVDLAAAADLAVDNGVVIDDHARTSDHNIVAAGDCASHDMARYGRRIrLESVPSAAEQAKVAAATICGKPKEIK-ALPWF 321
Cdd:COG1251 241 NTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRV-LELVAPAYEQARVAAANLAGGPAAYEgSVPST 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1132153779 322 WSDQYDFKLQIAGLNTGYDEVVLSGNPTRDSdFTCYYLRSAELIAADCINRPRDFMFSKRVITQQLPIDRAEL 394
Cdd:COG1251 320 KLKVFGVDVASAGDAEGDEEVVVRGDPARGV-YKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRAL 391
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
24-334 |
1.79e-91 |
|
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: 278.23 E-value: 1.79e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 24 QERWTGEIVLIGDESALPYQRPPLSKAYLASKSTLKDLEIRSVEFYSKHGIQLR-DATVEAIDRSAGSLSLSTGDALTYD 102
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRDGETLSYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 103 KLALCTGARPRRLPTPGADLAGVYYLRTAADVGLIRKA--ANPGRRAVIVGGGYIGLETAASLRALGLEVTVLEATERVL 180
Cdd:COG0446 81 KLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREAlkEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 181 ERVtAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRVReVVLASGESIPADLLIIGIGVEPNVDLAAAA--DLAVDNGV 258
Cdd:COG0446 161 GVL-DPEMAALLEEELREHGVELRLGETVVAIDGDDKVA-VTLTDGEEIPADLVVVAPGVRPNTELAKDAglALGERGWI 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1132153779 259 VIDDHARTSDHNIVAAGDCASHDMARYGRRIRLESVPSAAEQAKVAAATICGKPKEIKALPWFWSDQYDFKLQIAG 334
Cdd:COG0446 239 KVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFDLCIASTG 314
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
1-395 |
3.11e-74 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 236.36 E-value: 3.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 1 MTAQRAVIIGASHAGAQLATSLRQERWTGEIVLIGDESALPYQRPPLSKAYLASKST-LKDLeiRSVEFYSKHGIQLRDA 79
Cdd:PRK09754 1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPqLQQV--LPANWWQENNVHLHSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 80 -TVEAIDRSAGSLSLSTGDALTYDKLALCTGARPRRLPTPGADLAGVYYLRTAADVGLIRKAANPGRRAVIVGGGYIGLE 158
Cdd:PRK09754 79 vTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 159 TAASLRALGLEVTVLEATERVLERVTAPEVSAFFDRIHRSKGVNI-RTGALVEALTGDSRVreVVLASGESIPADLLIIG 237
Cdd:PRK09754 159 LAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRIlLNNAIEHVVDGEKVE--LTLQSGETLQADVVIYG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 238 IGVEPNVDLAAAADLAVDNGVVIDDHARTSDHNIVAAGDCASHDMARyGRRIRLESVPSAAEQAKVAAATICGKPKEIKA 317
Cdd:PRK09754 237 IGISANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDN-GALHRCESWENANNQAQIAAAAMLGLPLPLLP 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1132153779 318 LPWFWSDQYDFKLQIAGlNTGYDEVVLSGNPTRDSDFtCYYLRSAELIAADCINRPRDFMFSKRVITQQLPIDRAELS 395
Cdd:PRK09754 316 PPWFWSDQYSDNLQFIG-DMRGDDWLCRGNPETQKAI-WFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLI 391
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
7-277 |
4.75e-66 |
|
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: 212.18 E-value: 4.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 7 VIIGASHAGAQLATSLRQERwtGEIVLIGDESALPYQRPPLSKAYLASKSTLKDLEIRS--VEFYSKH------GIQLR- 77
Cdd:pfam07992 4 VVIGGGPAGLAAALTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWAdlYKRKEEVvkklnnGIEVLl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 78 DATVEAIDRSAGSLSLST-----GDALTYDKLALCTGARPRRLPTPGADLAGVYYLRTAADVGLIRKAANPGRrAVIVGG 152
Cdd:pfam07992 82 GTEVVSIDPGAKKVVLEElvdgdGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKR-VVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 153 GYIGLETAASLRALGLEVTVLEATERVLeRVTAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLASGESIPAD 232
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDAD 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1132153779 233 LLIIGIGVEPNVDLAAAA--DLAVDNGVVIDDHARTSDHNIVAAGDC 277
Cdd:pfam07992 240 LVVVAIGRRPNTELLEAAglELDERGGIVVDEYLRTSVPGIYAAGDC 286
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
7-286 |
4.50e-48 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 174.63 E-value: 4.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 7 VIIGASHAGAQLATSLRQ-ERWTGEIVLIGDESALPYQRPPLSKaYLASKSTLKDLEIRSVEFYSKHGIQL-RDATVEAI 84
Cdd:TIGR02374 2 VLVGNGMAGHRCIEEVLKlNRHMFEITIFGEEPHPNYNRILLSS-VLQGEADLDDITLNSKDWYEKHGITLyTGETVIQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 85 DRSAGSLSLSTGDALTYDKLALCTGARPRRLPTPGADLAGVYYLRTAADVGLIRKAANPGRRAVIVGGGYIGLETAASLR 164
Cdd:TIGR02374 81 DTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 165 ALGLEVTVLEATERVLERVTAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLASGESIPADLLIIGIGVEPNV 244
Cdd:TIGR02374 161 NLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1132153779 245 DLAAAADLAVDNGVVIDDHARTSDHNIVAAGDCASHDMARYG 286
Cdd:TIGR02374 241 ELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYG 282
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
5-279 |
6.79e-38 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 140.65 E-value: 6.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 5 RAVIIGASHAGAQLATSLRQERWTG-EIVLIGDESALPYQrpPLSKAYLASKSTLKDLEIRSVEFYSKHGIQLRDATVEA 83
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKKLGGDaEVTLIDPNPYHLFQ--PLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 84 IDRSAGSLSLSTGDALTYDKLALCTGARPRRLPTPGAD--------LAGVYYLRTAADVGLIRKAANPGRRAVIVGGGYI 155
Cdd:COG1252 81 IDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAehalplktLEDALALRERLLAAFERAERRRLLTIVVVGGGPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 156 GLETAASLRAL-------------GLEVTVLEATERVLERVtAPEVSAFFDRIHRSKGVNIRTGALVEALTGDsrvrEVV 222
Cdd:COG1252 161 GVELAGELAELlrkllrypgidpdKVRITLVEAGPRILPGL-GEKLSEAAEKELEKRGVEVHTGTRVTEVDAD----GVT 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1132153779 223 LASGESIPADLLIIGIGVEPNVDLAAAADLAVDNG-VVIDDHARTSDH-NIVAAGDCAS 279
Cdd:COG1252 236 LEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGrVLVDPTLQVPGHpNVFAIGDCAA 294
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
64-283 |
1.14e-36 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 138.63 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 64 RSVEFYSKHGIQLRDAT-VEAIDRSAGSL---SLSTGDAL--TYDKLALCTGARPRRLPTPGADLAGVYYLRTAADVGLI 137
Cdd:PRK09564 61 RTPEEFIKSGIDVKTEHeVVKVDAKNKTItvkNLKTGSIFndTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 138 RKAANPGR--RAVIVGGGYIGLETAASLRALGLEVTVLEATERVLERVTAPEVSAFFDRIHRSKGVNIRTGALVEALTGD 215
Cdd:PRK09564 141 KELLKDEEikNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGE 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1132153779 216 SRVREVVLASGEsIPADLLIIGIGVEPNVDLAAAAD-LAVDNG-VVIDDHARTSDHNIVAAGDCAS-HDMA 283
Cdd:PRK09564 221 DKVEGVVTDKGE-YEADVVIVATGVKPNTEFLEDTGlKTLKNGaIIVDEYGETSIENIYAAGDCATiYNIV 290
|
|
| Reductase_C |
pfam14759 |
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ... |
320-394 |
1.28e-29 |
|
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: 109.58 E-value: 1.28e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1132153779 320 WFWSDQYDFKLQIAGLNTGYDEVVLSGNPtRDSDFTCYYLRSAELIAADCINRPRDFMFSKRVITQQLPIDRAEL 394
Cdd:pfam14759 1 WFWSDQYDLKLQIAGLPTGADEVVLRGDP-EDGAFSVFYLRDGRLVAVDAVNRPRDFMAARRLIARGASVDPAAL 74
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
7-278 |
2.35e-28 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 114.24 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 7 VIIGASHAGAQLATSLRQERWTGEIVLIGDESALPYQRPPLSKAYlaSKSTLKDLEIRSV--EFYSKHGIQLRDAT-VEA 83
Cdd:PRK04965 6 VIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVF--SQGQRADDLTRQSagEFAEQFNLRLFPHTwVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 84 IDRSAGSLsLSTGDALTYDKLALCTGARPRRLPTPGADLagVYYLRTAADVGLIRKAANPGRRAVIVGGGYIGLETAASL 163
Cdd:PRK04965 84 IDAEAQVV-KSQGNQWQYDKLVLATGASAFVPPIPGREL--MLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 164 RALGLEVTVLEATERVLERVTAPEVSAFFDRIHRSKGVNIRTGALVEALT-GDSRVReVVLASGESIPADLLIIGIGVEP 242
Cdd:PRK04965 161 CRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEkTDSGIR-ATLDSGRSIEVDAVIAAAGLRP 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 1132153779 243 NVDLAAAADLAVDNGVVIDDHARTSDHNIVAAGDCA 278
Cdd:PRK04965 240 NTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCA 275
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
1-286 |
4.11e-28 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 116.76 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 1 MTAQRAVIIGASHAGAQLATSL--RQERWTGEIVLIGDESALPYQRPPLSKAYlaSKSTLKDLEIRSVEFYSKHGIQ-LR 77
Cdd:PRK14989 1 MSKVRLAIIGNGMVGHRFIEDLldKADAANFDITVFCEEPRIAYDRVHLSSYF--SHHTAEELSLVREGFYEKHGIKvLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 78 DATVEAIDRSAGSLSLSTGDALTYDKLALCTGARPRRLPTPGADLAGVYYLRTAADVGLIRKAANPGRRAVIVGGGYIGL 157
Cdd:PRK14989 79 GERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 158 ETAASLRALGLEVTVLEATERVLERVTAPEVSAFFDRIHRSKGVNIRTGALVEALT--GDSRVREVVLASGESIPADLLI 235
Cdd:PRK14989 159 EAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqeGVEARKTMRFADGSELEVDFIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1132153779 236 IGIGVEPN--VDLAAAADLAVDNGVVIDDHARTSDHNIVAAGDCASHDMARYG 286
Cdd:PRK14989 239 FSTGIRPQdkLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFG 291
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
65-282 |
5.79e-27 |
|
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: 111.72 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 65 SVEFYSKHGIQLRDATVEAIDrsAGSLSLSTGDALTYDKLALCTGARPRRLPTPGADlaGVYYLrTAADVGLIRKaanPG 144
Cdd:COG1249 97 VEELLKKNGVDVIRGRARFVD--PHTVEVTGGETLTADHIVIATGSRPRVPPIPGLD--EVRVL-TSDEALELEE---LP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 145 RRAVIVGGGYIGLETAASLRALGLEVTVLEATERVLERVTaPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLA 224
Cdd:COG1249 169 KSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGED-PEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLE 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1132153779 225 SG---ESIPADLLIIGIGVEPNVDL----AAAADLAVDNGVVIDDHARTSDHNIVAAGDCASHDM 282
Cdd:COG1249 248 DGggeEAVEADKVLVATGRRPNTDGlgleAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQ 312
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
71-280 |
1.92e-24 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 102.12 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 71 KHGIQLRDATVEAIDRSAGSLSLSTGDALTY--DKLALCTGARPRRLPTPGADLA---GVYYLRTAadvgliRKAANPGR 145
Cdd:COG0492 69 RFGAEILLEEVTSVDKDDGPFRVTTDDGTEYeaKAVIIATGAGPRKLGLPGEEEFegrGVSYCATC------DGFFFRGK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 146 RAVIVGGGYIGLETAASLRALGLEVTVLeaTERvlERVTAPEVSAffDRIHRSKGVNIRTGALVEALTGDSRVREVVLAS 225
Cdd:COG0492 143 DVVVVGGGDSALEEALYLTKFASKVTLI--HRR--DELRASKILV--ERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKN 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1132153779 226 GES-----IPADLLIIGIGVEPNV--DLAAAADLAVDNGVVIDDHARTSDHNIVAAGDCASH 280
Cdd:COG0492 217 VKTgeekeLEVDGVFVAIGLKPNTelLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY 278
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
96-277 |
4.80e-22 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 97.58 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 96 GDALTYDKLALCTGARPRRLPTPGadLAGVYYLRTAADVGLIRKaanPgRRAVIVGGGYIGLETAASLRALGLEVTVLEA 175
Cdd:PRK06370 129 GETLRAKRIFINTGARAAIPPIPG--LDEVGYLTNETIFSLDEL---P-EHLVIIGGGYIGLEFAQMFRRFGSEVTVIER 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 176 TERVLERvTAPEVSAFFDRIHRSKGVNIRTGALVEAL--TGDSRVREVVLASGE-SIPADLLIIGIGVEPNVDL----AA 248
Cdd:PRK06370 203 GPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVerDGDGIAVGLDCNGGApEITGSHILVAVGRVPNTDDlgleAA 281
|
170 180
....*....|....*....|....*....
gi 1132153779 249 AADLAVDNGVVIDDHARTSDHNIVAAGDC 277
Cdd:PRK06370 282 GVETDARGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
106-276 |
2.07e-21 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 95.60 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 106 LCTGARPRRLPtpGADLAGvyylRTaadVGLIRKAANPGR---RAVIVGGGYIGLETAASLRALGLEVTVLEATERVLEr 182
Cdd:PRK06416 140 LATGSRPRELP--GIEIDG----RV---IWTSDEALNLDEvpkSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILP- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 183 VTAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLASG---ESIPADLLIIGIGVEPNVDLAaaadlavdnG-- 257
Cdd:PRK06416 210 GEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVTVTLEDGgkeETLEADYVLVAVGRRPNTENL---------Gle 280
|
170 180
....*....|....*....|....*....
gi 1132153779 258 ----------VVIDDHARTSDHNIVAAGD 276
Cdd:PRK06416 281 elgvktdrgfIEVDEQLRTNVPNIYAIGD 309
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
146-226 |
6.38e-20 |
|
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: 83.41 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 146 RAVIVGGGYIGLETAASLRALGLEVTVLEATERVLeRVTAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLAS 225
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
.
gi 1132153779 226 G 226
Cdd:pfam00070 80 G 80
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
91-279 |
3.58e-19 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 88.86 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 91 LSLSTGDALTYDKLALCTGARPRRLPTPGadLAGVYYlRTAADVglIRKAANPgRRAVIVGGGYIGLETAASLRALGLEV 170
Cdd:PRK07846 119 LRTGDGEEITADQVVIAAGSRPVIPPVIA--DSGVRY-HTSDTI--MRLPELP-ESLVIVGGGFIAAEFAHVFSALGVRV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 171 TVLEATERVLeRVTAPEVSAFFDRIHRSKgVNIRTGALVEALTGDSRVREVVLASGESIPADLLIIGIGVEPNVDLAAAA 250
Cdd:PRK07846 193 TVVNRSGRLL-RHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNGDLLDAA 270
|
170 180 190
....*....|....*....|....*....|...
gi 1132153779 251 DL---AVDNG-VVIDDHARTSDHNIVAAGDCAS 279
Cdd:PRK07846 271 AAgvdVDEDGrVVVDEYQRTSAEGVFALGDVSS 303
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
102-277 |
1.69e-17 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 83.69 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 102 DKLALCTGARprRLPTPGADLA-GVYYLRTaadVGLIRKAANPGRRAVIvGGGYIGLETAASLRALGLEVTVLEATERVL 180
Cdd:PRK06292 132 KNIVIATGSR--VPPIPGVWLIlGDRLLTS---DDAFELDKLPKSLAVI-GGGVIGLELGQALSRLGVKVTVFERGDRIL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 181 eRVTAPEVSAFFDRIHrSKGVNIRTGALVEALTGDSRVREVVLASG---ESIPADLLIIGIGVEPNVDLAAAAD---LAV 254
Cdd:PRK06292 206 -PLEDPEVSKQAQKIL-SKEFKIKLGAKVTSVEKSGDEKVEELEKGgktETIEADYVLVATGRRPNTDGLGLENtgiELD 283
|
170 180
....*....|....*....|....
gi 1132153779 255 DNG-VVIDDHARTSDHNIVAAGDC 277
Cdd:PRK06292 284 ERGrPVVDEHTQTSVPGIYAAGDV 307
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
65-276 |
1.06e-15 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 78.25 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 65 SVEFYSKHGIQLRDATVEAidrSAGSLSLStgdaLTYDKLALCTGARPRRLPTPG-ADLAGVYylrtaADVGLIRKAANP 143
Cdd:PRK07251 90 GVDLYDAEAHFVSNKVIEV---QAGDEKIE----LTAETIVINTGAVSNVLPIPGlADSKHVY-----DSTGIQSLETLP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 144 GRRAVIvGGGYIGLETAASLRALGLEVTVLEATERVLERVtAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRvREVVL 223
Cdd:PRK07251 158 ERLGII-GGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE-EPSVAALAKQYMEEDGITFLLNAHTTEVKNDGD-QVLVV 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1132153779 224 ASGESIPADLLIIGIGVEPNVDLA----AAADLAVDNGVVIDDHARTSDHNIVAAGD 276
Cdd:PRK07251 235 TEDETYRFDALLYATGRKPNTEPLglenTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
101-279 |
2.60e-15 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 77.10 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 101 YDKLALCTGA-RPRRLPTPGADLAGVY----YLRTAADVGLIRKAANPGRRAVIVGGGYIGLETAASLRALG-LEVTvle 174
Cdd:COG0493 207 FDAVFLATGAgKPRDLGIPGEDLKGVHsamdFLTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVT--- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 175 aterVLERVTAPEVSAFFDRIHRSK--GVNIRTGALVEALTGDS--RVREVVL---------ASG-----------ESIP 230
Cdd:COG0493 284 ----IVYRRTREEMPASKEEVEEALeeGVEFLFLVAPVEIIGDEngRVTGLECvrmelgepdESGrrrpvpiegseFTLP 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1132153779 231 ADLLIIGIGVEPNVDLAAAADLAVDNG---VVIDDHA-RTSDHNIVAAGDCAS 279
Cdd:COG0493 360 ADLVILAIGQTPDPSGLEEELGLELDKrgtIVVDEETyQTSLPGVFAGGDAVR 412
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
1-276 |
2.86e-15 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 76.98 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 1 MTAQRAVIIGASHAGAQLATSLRQERWTgeiVLIGDESALPYQRPPLSKAYLASKSTLKDLE------------------ 62
Cdd:PRK08010 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWR---VALIEQSNAMYGGTCINIGCIPTKTLVHDAQqhtdfvraiqrknevvnf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 63 IRSVEFYS---KHGIQLRDATVEAIDRSAGSLSLSTGD-ALTYDKLALCTGARPRRLPTPG-ADLAGVYylrtaADVGLI 137
Cdd:PRK08010 78 LRNKNFHNladMPNIDVIDGQAEFINNHSLRVHRPEGNlEIHGEKIFINTGAQTVVPPIPGiTTTPGVY-----DSTGLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 138 RKAANPGRRAvIVGGGYIGLETAASLRALGLEVTVLEATERVLERvTAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSR 217
Cdd:PRK08010 153 NLKELPGHLG-ILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHEN 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1132153779 218 VREVVLASGESIpADLLIIGIGVEPNVDLAAAADLAVD----NGVVIDDHARTSDHNIVAAGD 276
Cdd:PRK08010 231 QVQVHSEHAQLA-VDALLIASGRQPATASLHPENAGIAvnerGAIVVDKYLHTTADNIWAMGD 292
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
4-279 |
8.71e-15 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 75.59 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 4 QRAVIIGASHAGAQLATSLRQERWTGEIVLIG---DES----ALPYqrpplskaYLAS--KSTLKDLEIRSVEFYSKHGI 74
Cdd:PRK13512 2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEkdrDMSfancALPY--------YIGEvvEDRKYALAYTPEKFYDRKQI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 75 QLR-----------DATVEAIDRSagslslsTGDALT--YDKLALCTGARPRRLPTpgaDLAGVYYLRTAADVGLIRK-- 139
Cdd:PRK13512 74 TVKtyheviaindeRQTVTVLNRK-------TNEQFEesYDKLILSPGASANSLGF---ESDITFTLRNLEDTDAIDQfi 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 140 AANPGRRAVIVGGGYIGLETAASLRALGLEVTVLEATERVLERVTAPEVSAFFDRIHrSKGVNIRTGALVEALTGDsrvr 219
Cdd:PRK13512 144 KANQVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELD-KREIPYRLNEEIDAINGN---- 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1132153779 220 EVVLASGESIPADLLIIGIGVEPNVDLAAAADLAVDNG--VVIDDHARTSDHNIVAAGDCAS 279
Cdd:PRK13512 219 EVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIIT 280
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
99-279 |
4.32e-14 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 73.26 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 99 LTYDKLALCTGARPRRLPTPGADlAGVYYLRTAADVGLIRK--------AANP------GRR---AVIVGGGYIGLETAA 161
Cdd:PTZ00318 112 VPYDKLVVAHGARPNTFNIPGVE-ERAFFLKEVNHARGIRKrivqcierASLPttsveeRKRllhFVVVGGGPTGVEFAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 162 SLRALGLE--------------VTVLEATERVLERVTApEVSAFFDRIHRSKGVNIRTGALVEALTGDsrvrEVVLASGE 227
Cdd:PTZ00318 191 ELADFFRDdvrnlnpelveeckVTVLEAGSEVLGSFDQ-ALRKYGQRRLRRLGVDIRTKTAVKEVLDK----EVVLKDGE 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1132153779 228 SIPADLLIIGIGVEPNVDLAAAADLAVDNG-VVIDDHARTSD-HNIVAAGDCAS 279
Cdd:PTZ00318 266 VIPTGLVVWSTGVGPGPLTKQLKVDKTSRGrISVDDHLRVKPiPNVFALGDCAA 319
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
95-277 |
1.76e-13 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 71.73 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 95 TGDALTYDKLALCTGARPRRLPTPGADLA----GVYYLRtaadvglirkaANPgRRAVIVGGGYIGLETAASLRALGLEV 170
Cdd:PRK06116 126 NGERYTADHILIATGGRPSIPDIPGAEYGitsdGFFALE-----------ELP-KRVAVVGAGYIAVEFAGVLNGLGSET 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 171 TVLEATERVLERvtapevsafFDRIHRS--------KGVNIRTGALVEAL--TGDSRVReVVLASGESIPADLLIIGIGV 240
Cdd:PRK06116 194 HLFVRGDAPLRG---------FDPDIREtlveemekKGIRLHTNAVPKAVekNADGSLT-LTLEDGETLTVDCLIWAIGR 263
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1132153779 241 EPNVDL---AAAADLAVDNG-VVIDDHARTSDHNIVAAGDC 277
Cdd:PRK06116 264 EPNTDGlglENAGVKLNEKGyIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
108-282 |
3.01e-13 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 71.11 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 108 TGARPRRLPtpGADLAGVyylRTAADVGLIRKAANPGRRAVIvGGGYIGLETAASLRALGLEVTVLEATERVLERV---T 184
Cdd:PRK06327 153 TGSEPRHLP--GVPFDNK---IILDNTGALNFTEVPKKLAVI-GAGVIGLELGSVWRRLGAEVTILEALPAFLAAAdeqV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 185 APEVSAFFDRihrsKGVNIRTGALVEAL-TGDSRVR-EVVLASGE--SIPADLLIIGIGVEPNVDLAAAAD---LAVDNG 257
Cdd:PRK06327 227 AKEAAKAFTK----QGLDIHLGVKIGEIkTGGKGVSvAYTDADGEaqTLEVDKLIVSIGRVPNTDGLGLEAvglKLDERG 302
|
170 180
....*....|....*....|....*.
gi 1132153779 258 -VVIDDHARTSDHNIVAAGDCASHDM 282
Cdd:PRK06327 303 fIPVDDHCRTNVPNVYAIGDVVRGPM 328
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
101-276 |
2.66e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 67.32 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 101 YDKLALCTGA-RPRRLPTPGADLAGVY----YL-RT-AADVGLIRKAANP---GRRAVIVGGGYIGLETAASLRALGLEV 170
Cdd:PRK12770 119 YDAVLIATGTwKSRKLGIPGEDLPGVYsaleYLfRIrAAKLGYLPWEKVPpveGKKVVVVGAGLTAVDAALEAVLLGAEK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 171 TVLeATERVLERvtAPEVSAFFDRIhRSKGVNIRTGALVEALTGDSRVREVVLA--------------------SGESIP 230
Cdd:PRK12770 199 VYL-AYRRTINE--APAGKYEIERL-IARGVEFLELVTPVRIIGEGRVEGVELAkmrlgepdesgrprpvpipgSEFVLE 274
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1132153779 231 ADLLIIGIGVEPN---VDLAAAADLAVDNGVVIDDHARTSDHNIVAAGD 276
Cdd:PRK12770 275 ADTVVFAIGEIPTppfAKECLGIELNRKGEIVVDEKHMTSREGVFAAGD 323
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
43-276 |
1.46e-11 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 65.56 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 43 QRPPLSKAYLASKSTLKDL----------EIRSVE-FYSKHGIQLRDATVEAIDrsAGSLSLSTGDA----LTYDKLALC 107
Cdd:PRK05249 67 QNPLYSSYRVKLRITFADLlaradhvinkQVEVRRgQYERNRVDLIQGRARFVD--PHTVEVECPDGevetLTADKIVIA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 108 TGARPRRlpTPGADLAGVYYLRTAADVGLIRKaanPgRRAVIVGGGYIGLETAASLRALGLEVTVLEATERVLERVTaPE 187
Cdd:PRK05249 145 TGSRPYR--PPDVDFDHPRIYDSDSILSLDHL---P-RSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLD-DE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 188 VSAFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLASGESIPAD--------------LLIIGIGVEPNVDlaaaadla 253
Cdd:PRK05249 218 ISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADcllyangrtgntdgLNLENAGLEADSR-------- 289
|
250 260
....*....|....*....|....
gi 1132153779 254 vdnG-VVIDDHARTSDHNIVAAGD 276
Cdd:PRK05249 290 ---GqLKVNENYQTAVPHIYAVGD 310
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
75-277 |
1.94e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 62.48 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 75 QLRDATVEAIDRSAGSLSLSTGDA-------------------LTYDKLALCTGARPRRLPTPGadLAGV-YYLRTAAdv 134
Cdd:PRK13748 188 ELRHAKYEGILDGNPAITVLHGEArfkddqtlivrlndggervVAFDRCLIATGASPAVPPIPG--LKETpYWTSTEA-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 135 gLIRKAAnPGRRAVIvGGGYIGLETAASLRALGLEVTVLeATERVL--------ERVTApevsAFfdrihRSKGVNIRTG 206
Cdd:PRK13748 264 -LVSDTI-PERLAVI-GSSVVALELAQAFARLGSKVTIL-ARSTLFfredpaigEAVTA----AF-----RAEGIEVLEH 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1132153779 207 ALVEALTGDSRvrEVVLASGE-SIPADLLIIGIGVEPNVDL----AAAADLAVDNGVVIDDHARTSDHNIVAAGDC 277
Cdd:PRK13748 331 TQASQVAHVDG--EFVLTTGHgELRADKLLVATGRAPNTRSlaldAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDC 404
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
101-278 |
2.08e-10 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 62.12 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 101 YDKLALCTGA-RPRRLPTPGADLAGVY----YLrTAADVGLIRKAANPGRRAVIVGGGYIGLETAASLRALGLE-VTVL- 173
Cdd:PRK11749 226 YDAVFIGTGAgLPRFLGIPGENLGGVYsavdFL-TRVNQAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAEsVTIVy 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 174 -----EATERVLERVTAPEvsaffdrihrsKGVNIRTGALVEALTGDS--------------------RVREVVLASGES 228
Cdd:PRK11749 305 rrgreEMPASEEEVEHAKE-----------EGVEFEWLAAPVEILGDEgrvtgvefvrmelgepdasgRRRVPIEGSEFT 373
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1132153779 229 IPADLLIIGIGVEPNVDLAAAADLAVDNG----VVIDDHARTSDHNIVAAGDCA 278
Cdd:PRK11749 374 LPADLVIKAIGQTPNPLILSTTPGLELNRwgtiIADDETGRTSLPGVFAGGDIV 427
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
95-277 |
5.64e-10 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 60.95 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 95 TGDAL--TYDKLALCTGA-RPRRLPTPGADLAGVY----YLRTAADVGLIRKAANP----GRRAVIVGGGyiglETAA-- 161
Cdd:PRK12810 221 TAEELlaEYDAVFLGTGAyKPRDLGIPGRDLDGVHfamdFLIQNTRRVLGDETEPFisakGKHVVVIGGG----DTGMdc 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 162 ---SLRaLG-LEVTVLEATERVLERVTAPEVSAFFDRIHRSK-----GVNIRTGALVEALTG-DSRVREVVLA------- 224
Cdd:PRK12810 297 vgtAIR-QGaKSVTQRDIMPMPPSRRNKNNPWPYWPMKLEVSnaheeGVEREFNVQTKEFEGeNGKVTGVKVVrtelgeg 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1132153779 225 -------SGESIPADLLIIGIGVEPNVDL--AAAADLAVDNGVVIDDHA--RTSDHNIVAAGDC 277
Cdd:PRK12810 376 dfepvegSEFVLPADLVLLAMGFTGPEAGllAQFGVELDERGRVAAPDNayQTSNPKVFAAGDM 439
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
73-276 |
1.01e-09 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 60.21 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 73 GIQLRDATVEAIDRSAGSLSLSTGDALTY--DKLALCTGARPRRLPTPGADLAgvyylrTAADVGLirKAANPGRRAVIV 150
Cdd:PLN02507 138 GVKLYEGEGKIVGPNEVEVTQLDGTKLRYtaKHILIATGSRAQRPNIPGKELA------ITSDEAL--SLEELPKRAVVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 151 GGGYIGLETAASLRALGLEVTVLEATERVLeRVTAPEVSAFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLASGESIP 230
Cdd:PLN02507 210 GGGYIAVEFASIWRGMGATVDLFFRKELPL-RGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFV 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1132153779 231 ADLLIIGIGVEPNVDLAAAADL----AVDNGVVIDDHARTSDHNIVAAGD 276
Cdd:PLN02507 289 ADVVLFATGRAPNTKRLNLEAVgvelDKAGAVKVDEYSRTNIPSIWAIGD 338
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
82-277 |
2.16e-09 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 59.24 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 82 EAIDRSAGSLSLSTGDALTYDKLALCTGARPRrlpTPgaDLAGVYYLRTAADVGLIRKAanpgRRAVIVGGGYIGLETAA 161
Cdd:PTZ00058 184 EVTIVSAGVSQLDDGQVIEGKNILIAVGNKPI---FP--DVKGKEFTISSDDFFKIKEA----KRIGIAGSGYIAVELIN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 162 SLRALGLEVTVLEATERVLERVTAPEVSAFFDRIHRSkGVNIRTGALVEALTGDSRVREVVLAS--GESIPADLLIIGIG 239
Cdd:PTZ00058 255 VVNRLGAESYIFARGNRLLRKFDETIINELENDMKKN-NINIITHANVEEIEKVKEKNLTIYLSdgRKYEHFDYVIYCVG 333
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1132153779 240 VEPNVDL---AAAADLAVDNGVVIDDHARTSDHNIVAAGDC 277
Cdd:PTZ00058 334 RSPNTEDlnlKALNIKTPKGYIKVDDNQRTSVKHIYAVGDC 374
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
85-278 |
4.31e-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: 54.86 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 85 DRSAGSLSLSTGDALTYDKLALCTGARPRRLPTPGADLAGVyylrTAADvgLIRKAANPGRrAVIVGGGYIGLETAASLR 164
Cdd:TIGR01438 128 HRIKATNKKGKEKIYSAERFLIATGERPRYPGIPGAKELCI----TSDD--LFSLPYCPGK-TLVVGASYVALECAGFLA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 165 ALGLEVTVLeaTERVLERVTAPEVSAFFDRIHRSKGVNIRTGALVEALTG-DSRVREVVLASGESIPA--DLLIIGIGVE 241
Cdd:TIGR01438 201 GIGLDVTVM--VRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQiEAKVLVEFTDSTNGIEEeyDTVLLAIGRD 278
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1132153779 242 P-----NVDLAAAADLAVDNGVVIDDHARTSDHNIVAAGDCA 278
Cdd:TIGR01438 279 ActrklNLENVGVKINKKTGKIPADEEEQTNVPYIYAVGDIL 320
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
47-282 |
6.69e-08 |
|
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: 54.21 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 47 LSKAYlasKSTLKDLEirSVEFYSKHGiQLRDATVEAIDRSAGSLSlSTGDALTYDKLALCTGARPRRLPTPGADLA--- 123
Cdd:TIGR01423 105 INKSY---EGMFADTE--GLTFFLGWG-ALEDKNVVLVRESADPKS-AVKERLQAEHILLATGSWPQMLGIPGIEHCiss 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 124 -GVYYLrtaadvglirkaANPGRRAVIVGGGYIGLETAA---SLRALGLEVTVLEATERVLeRVTAPEVSAFFDRIHRSK 199
Cdd:TIGR01423 178 nEAFYL------------DEPPRRVLTVGGGFISVEFAGifnAYKPRGGKVTLCYRNNMIL-RGFDSTLRKELTKQLRAN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 200 GVNIRTG---ALVEALTGDSrvREVVLASGESIPADLLIIGIGVEPNVDLAAAADL----AVDNGVVIDDHARTSDHNIV 272
Cdd:TIGR01423 245 GINIMTNenpAKVTLNADGS--KHVTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVgvelTKKGAIQVDEFSRTNVPNIY 322
|
250
....*....|
gi 1132153779 273 AAGDCASHDM 282
Cdd:TIGR01423 323 AIGDVTDRVM 332
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
2-279 |
1.94e-07 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 53.19 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 2 TAQRAVIIGASHAGAQLATSLRQErwtGEIVLIGDES---------ALPYQRPPlskaylaskSTLKDLEIRSVEfysKH 72
Cdd:PRK12814 192 SGKKVAIIGAGPAGLTAAYYLLRK---GHDVTIFDANeqaggmmryGIPRFRLP---------ESVIDADIAPLR---AM 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 73 GIQLRDATVEAIDRSAGSLSLStgdaltYDKLALCTGA-RPRRLPTPGADLAGVY----YLRTAADvgliRKAANPGRRA 147
Cdd:PRK12814 257 GAEFRFNTVFGRDITLEELQKE------FDAVLLAVGAqKASKMGIPGEELPGVIsgidFLRNVAL----GTALHPGKKV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 148 VIVGGGYIGLETAASLRALGLE-VTVL-------------EATERVLERVTAPEVSAFFDrIHRSKG------VNIRTGA 207
Cdd:PRK12814 327 VVIGGGNTAIDAARTALRLGAEsVTILyrrtreempanraEIEEALAEGVSLRELAAPVS-IERSEGgleltaIKMQQGE 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1132153779 208 LVEAltgdSRVREVVLASGE-SIPADLLIIGIG--VEPNVDLAAAADLAVDNGVVIDDHA-RTSDHNIVAAGDCAS 279
Cdd:PRK12814 406 PDES----GRRRPVPVEGSEfTLQADTVISAIGqqVDPPIAEAAGIGTSRNGTVKVDPETlQTSVAGVFAGGDCVT 477
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
63-278 |
8.26e-06 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 47.90 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 63 IRSVEFYSKHGiqLRDATVEAIDRSAgSL----SLSTGD-----ALTYDKLALCTGARPRrLP--TPGAdlagVYYLRTA 131
Cdd:PTZ00052 101 IRSLNFSYRTG--LRSSKVEYINGLA-KLkdehTVSYGDnsqeeTITAKYILIATGGRPS-IPedVPGA----KEYSITS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 132 ADVGLIRKaaNPGRrAVIVGGGYIGLETAASLRALGLEVTVL--EATERVLERVTAPEVSAFFdrihRSKGVNIRTGALV 209
Cdd:PTZ00052 173 DDIFSLSK--DPGK-TLIVGASYIGLETAGFLNELGFDVTVAvrSIPLRGFDRQCSEKVVEYM----KEQGTLFLEGVVP 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1132153779 210 EALT-GDSRVReVVLASGESIPADLLIIGIGVEPNVDL----AAAADLAVDNGVVIDDHArTSDHNIVAAGDCA 278
Cdd:PTZ00052 246 INIEkMDDKIK-VLFSDGTTELFDTVLYATGRKPDIKGlnlnAIGVHVNKSNKIIAPNDC-TNIPNIFAVGDVV 317
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
95-277 |
9.12e-06 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 47.55 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 95 TGDALTYDKLALCTGARPRRLPTPGADlaG--------VYYLRTAADvglirkaanpgrRAVIVGGGYIGLETAASLRAL 166
Cdd:PRK07845 134 GEETLDADVVLIATGASPRILPTAEPD--GeriltwrqLYDLDELPE------------HLIVVGSGVTGAEFASAYTEL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 167 GLEVTVLEATERVL--ERVTAPEVsafFDRIHRSKGVNI----------RTGALVEALTGDSRVRE---VVLASGeSIP- 230
Cdd:PRK07845 200 GVKVTLVSSRDRVLpgEDADAAEV---LEEVFARRGMTVlkrsraesveRTGDGVVVTLTDGRTVEgshALMAVG-SVPn 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1132153779 231 -ADLLIIGIGVEPNvdlaaaadlaVDNGVVIDDHARTSDHNIVAAGDC 277
Cdd:PRK07845 276 tAGLGLEEAGVELT----------PSGHITVDRVSRTSVPGIYAAGDC 313
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
143-179 |
1.71e-05 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 46.84 E-value: 1.71e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1132153779 143 PGRRAVIVGGGYIGLETAASLRALGLEVTVLEATERV 179
Cdd:COG1231 6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRV 42
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
145-235 |
3.12e-05 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 45.70 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 145 RRAVIVGGGYIGLETAASLRALGLEVTVLEA--------------------------TERVLERVTAPEVSAFFDR---- 194
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVERappprpdgrgialsprslellrrlglWDRLLARGAPIRGIRVRDGsdgr 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 195 -----------------IHRSK------------GVNIRTGALVEALTGDSRVREVVLASGESIPADLLI 235
Cdd:COG0654 84 vlarfdaaetglpaglvVPRADleralleaaralGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVV 153
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
149-214 |
4.05e-05 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 45.68 E-value: 4.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1132153779 149 IVGGGYIGLETAASLRALGLEVTVLEATERVLERVTApEVSAFFDRIH-RSKGVNIRTGALVEALTG 214
Cdd:PTZ00153 317 IVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLDA-DVAKYFERVFlKSKPVRVHLNTLIEYVRA 382
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
101-276 |
4.29e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 45.39 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 101 YDKLALCTGA-RPRRLPTPGADLAGVYylrtAADVGLIR----KAANP--------GRRAVIVGGGYIGLETAASLRALG 167
Cdd:PRK12831 229 FDAVFIGSGAgLPKFMGIPGENLNGVF----SANEFLTRvnlmKAYKPeydtpikvGKKVAVVGGGNVAMDAARTALRLG 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 168 LEVTVL------EATERVLERVTAPEVSAFFD------RIH-----RSKGVNIRTGALVEA-LTGDSRVREVvlaSGES- 228
Cdd:PRK12831 305 AEVHIVyrrseeELPARVEEVHHAKEEGVIFDlltnpvEILgdengWVKGMKCIKMELGEPdASGRRRPVEI---EGSEf 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1132153779 229 -IPADLLIIGIGVEPNVDLAAAADLAVDNG----VVIDDHARTSDHNIVAAGD 276
Cdd:PRK12831 382 vLEVDTVIMSLGTSPNPLISSTTKGLKINKrgciVADEETGLTSKEGVFAGGD 434
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
148-235 |
5.50e-05 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 44.93 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 148 VIVGGGYIGLETAASLRALGLEVTVLE---------------------ATERVLE------RVTAPEVS----------- 189
Cdd:PRK09126 7 VVVGAGPAGLSFARSLAGSGLKVTLIErqplaaladpafdgreialthASREILQrlgawdRIPEDEISplrdakvlngr 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1132153779 190 ----------------------------AFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLASGESIPADLLI 235
Cdd:PRK09126 87 spfaltfdargrgadalgylvpnhlirrAAYEAVSQQDGIELLTGTRVTAVRTDDDGAQVTLANGRRLTARLLV 160
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
101-276 |
1.02e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 44.35 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 101 YDKLALCTGA-RPRRLPTPGADLAGVY----YLrtaADVGLIrKAANP--------GRRAVIVGGGYIGLETAASLRALG 167
Cdd:PRK12778 518 FKGIFIASGAgLPNFMNIPGENSNGVMssneYL---TRVNLM-DAASPdsdtpikfGKKVAVVGGGNTAMDSARTAKRLG 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 168 LEVTVLeatervLERVTAPEVSAFFDRIHRSK--GVNIRT-GALVEAL-TGDSRVREVVL---------ASG-------- 226
Cdd:PRK12778 594 AERVTI------VYRRSEEEMPARLEEVKHAKeeGIEFLTlHNPIEYLaDEKGWVKQVVLqkmelgepdASGrrrpvaip 667
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1132153779 227 ---ESIPADLLIIGIGVEPNVDLAAAADLAVDN---GVVIDDHARTSDHNIVAAGD 276
Cdd:PRK12778 668 gstFTVDVDLVIVSVGVSPNPLVPSSIPGLELNrkgTIVVDEEMQSSIPGIYAGGD 723
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
81-277 |
1.47e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 43.99 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 81 VEAIDRSAG--SLSLSTGDALTYDKLALCTGARPRRLPTPGADL---AGVYYLrtaadvglirkaanP--------GRRA 147
Cdd:PRK15317 289 ASKLEPAAGliEVELANGAVLKAKTVILATGARWRNMNVPGEDEyrnKGVAYC--------------PhcdgplfkGKRV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 148 VIVGGGYIGLETAASLRALGLEVTVLEatervlervTAPEVSA---FFDRIHRSKGVNIRTGALVEALTGD-SRVREVVL 223
Cdd:PRK15317 355 AVIGGGNSGVEAAIDLAGIVKHVTVLE---------FAPELKAdqvLQDKLRSLPNVTIITNAQTTEVTGDgDKVTGLTY 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 224 ---ASGES--IPADLLIIGIGVEPNVDLAAAADLAVDNG-VVIDDHARTSDHNIVAAGDC 277
Cdd:PRK15317 426 kdrTTGEEhhLELEGVFVQIGLVPNTEWLKGTVELNRRGeIIVDARGATSVPGVFAAGDC 485
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
20-232 |
1.94e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 42.98 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 20 TSLRQERWT-GEIVLIGDES--ALPYQRPPLSKA----YLASKSTLKDLEIRsvefyskhgiqlRDATVEAIDRSAGSLS 92
Cdd:pfam13738 42 PSFTSNGFGiPDLNAISPGTspAFTFNREHPSGNeyaeYLRRVADHFELPIN------------LFEEVTSVKKEDDGFV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 93 LST-GDALTYDKLALCTG--ARPRRLPTPgaDLAGVY-YLRTAADVglirkaanPGRRAVIVGGGYIGLETAASLRALGL 168
Cdd:pfam13738 110 VTTsKGTYQARYVIIATGefDFPNKLGVP--ELPKHYsYVKDFHPY--------AGQKVVVIGGYNSAVDAALELVRKGA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 169 EVTVLEATERVLERVTAPEVS------AFFDRIHRSKGVNIRTGALVEALTGDSRVREVVLASGESIPAD 232
Cdd:pfam13738 180 RVTVLYRGSEWEDRDSDPSYSlspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVSYKVHTEDGRKVTSN 249
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
145-175 |
4.30e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 42.20 E-value: 4.30e-04
10 20 30
....*....|....*....|....*....|.
gi 1132153779 145 RRAVIVGGGYIGLETAASLRALGLEVTVLEA 175
Cdd:COG0665 3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLER 33
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
140-239 |
4.71e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 42.16 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 140 AANPGRRAVIVGGGYIGLETAASLRALGLEVTVLEATERV-----LER---------------------------VTAPE 187
Cdd:COG2072 2 AATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVggtwrDNRypglrldtpshlyslpffpnwsddpdfPTGDE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1132153779 188 VSAFFDRIHRSKGV--NIRTGALVEALTGDSRVR--EVVLASGESIPADLLIIGIG 239
Cdd:COG2072 82 ILAYLEAYADKFGLrrPIRFGTEVTSARWDEADGrwTVTTDDGETLTARFVVVATG 137
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
139-179 |
7.37e-04 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 41.54 E-value: 7.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1132153779 139 KAANPGRRAVIVGGGYIGLETAASLRA-LGLEVTVLEATERV 179
Cdd:PLN02576 7 SAAASSKDVAVVGAGVSGLAAAYALASkHGVNVLVTEARDRV 48
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
136-209 |
8.65e-04 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 41.32 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 136 LIRKAANPGRRAVIVGGGYIGLETAASLRALGLEVTVLEATER---VLE----------RVTAPEVsaffDRIhRSKGVN 202
Cdd:PRK11749 132 LFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKaggLLRygipefrlpkDIVDREV----ERL-LKLGVE 206
|
....*..
gi 1132153779 203 IRTGALV 209
Cdd:PRK11749 207 IRTNTEV 213
|
|
| PRK07236 |
PRK07236 |
hypothetical protein; Provisional |
143-229 |
1.05e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235980 [Multi-domain] Cd Length: 386 Bit Score: 41.06 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 143 PGRRAVIVGGGYIGLETAASLRALGLEVTVLEATERVLER-----VTAPEVSAFFDRihrskgvniRTGALVEALTGDSR 217
Cdd:PRK07236 5 SGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERSPTELDGrgagiVLQPELLRALAE---------AGVALPADIGVPSR 75
|
90
....*....|..
gi 1132153779 218 VREVVLASGESI 229
Cdd:PRK07236 76 ERIYLDRDGRVV 87
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
145-179 |
1.05e-03 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 40.97 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....*
gi 1132153779 145 RRAVIVGGGYIGLETAASLRALGLEVTVLEATERV 179
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRV 36
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
146-179 |
1.14e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 40.84 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|....
gi 1132153779 146 RAVIVGGGYIGLETAASLRALGLEVTVLEATERV 179
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDP 34
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
143-179 |
1.29e-03 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 40.61 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1132153779 143 PGRRAVIVGGGYIGLETAASLRALGLEVTVLEATERV 179
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRL 38
|
|
| PRK07364 |
PRK07364 |
FAD-dependent hydroxylase; |
148-201 |
1.53e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236001 [Multi-domain] Cd Length: 415 Bit Score: 40.39 E-value: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1132153779 148 VIVGGGYIGLETAASLRALGLEVTVLEAT--ERVLERVTAPEVSAFFDRIHRSKGV 201
Cdd:PRK07364 22 AIVGGGIVGLTLAAALKDSGLRIALIEAQpaEAAAAKGQAYALSLLSARIFEGIGV 77
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
145-179 |
1.73e-03 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 40.22 E-value: 1.73e-03
10 20 30
....*....|....*....|....*....|....*
gi 1132153779 145 RRAVIVGGGYIGLETAASLRALGLEVTVLEATERV 179
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTP 38
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
138-179 |
1.75e-03 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 40.60 E-value: 1.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1132153779 138 RKAANPGRRAVIVGGGYIGLETAASLRALGLEVTVLEATERV 179
Cdd:PRK01747 254 RPGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAP 295
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
144-233 |
2.05e-03 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 40.62 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 144 GRRAVIVGGGYIGLETAASLRALGLEVTVLEATERVLERVtapevsaFFDRIHRSK----GVNIRTGalVEA-------- 211
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRV-------YTDRSSLSVpvdlGASIITG--VEAdvaterrp 763
|
90 100 110
....*....|....*....|....*....|....*...
gi 1132153779 212 ----------------LTGDSRVREVVlaSGESIPADL 233
Cdd:PLN02976 764 dpsslicaqlgleltvLNSDCPLYDVV--TGEKVPADL 799
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
101-279 |
2.30e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 40.24 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 101 YDKLALCTGA-RPRRLPTPGADLAGVY----YLRTAADVGLIRKaanpGRRAVIVGGGYIGLETAASLRALGLEvtvlEA 175
Cdd:PRK12771 223 FDAVFVAIGAqLGKRLPIPGEDAAGVLdavdFLRAVGEGEPPFL----GKRVVVIGGGNTAMDAARTARRLGAE----EV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 176 TerVLERVTAPEVSAFFDRIH--RSKGVNIRTG-ALVEALTGDSRVREVVLA----------------SGES--IPADLL 234
Cdd:PRK12771 295 T--IVYRRTREDMPAHDEEIEeaLREGVEINWLrTPVEIEGDENGATGLRVItvekmeldedgrpspvTGEEetLEADLV 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1132153779 235 IIGIG--VEPNVDLAAAADLAVDNGVVIDDHARTSDH-NIVAAGDCAS 279
Cdd:PRK12771 373 VLAIGqdIDSAGLESVPGVEVGRGVVQVDPNFMMTGRpGVFAGGDMVP 420
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
146-181 |
3.81e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 39.11 E-value: 3.81e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1132153779 146 RAVIVGGGYIGLETAASLRALGLEVTVLEATERVLE 181
Cdd:PRK07538 2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEAAPELRP 37
|
|
| AdoHcyase_NAD |
smart00997 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
144-174 |
5.15e-03 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 37.43 E-value: 5.15e-03
10 20 30
....*....|....*....|....*....|.
gi 1132153779 144 GRRAVIVGGGYIGLETAASLRALGLEVTVLE 174
Cdd:smart00997 23 GKNVVVAGYGDVGKGVAARLRGLGARVIVTE 53
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
103-278 |
8.19e-03 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 38.66 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 103 KLALCTGA-RPRRLPTPGADLAGV-----YYLRTAADVGLIRKAANP-----GRRAVIVGGGYIGLETAASLRALGLEVT 171
Cdd:PRK12779 395 KIFVGTGAgLPTFMNVPGEHLLGVmsaneFLTRVNLMRGLDDDYETPlpevkGKEVFVIGGGNTAMDAARTAKRLGGNVT 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132153779 172 vleaterVLERVTAPEVSAFFDRIHRS--KGVNIR-----------------TGALVEALT-----GDSRVREVVLASGE 227
Cdd:PRK12779 475 -------IVYRRTKSEMPARVEELHHAleEGINLAvlraprefigddhthfvTHALLDVNElgepdKSGRRSPKPTGEIE 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1132153779 228 SIPADLLIIGIGVEPNVDLAAAADLAVDNG----VVIDDHARTSDHNIVAAGDCA 278
Cdd:PRK12779 548 RVPVDLVIMALGNTANPIMKDAEPGLKTNKwgtiEVEKGSQRTSIKGVYSGGDAA 602
|
|
| |
