|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
4-403 |
1.28e-150 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 431.87 E-value: 1.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 4 RLVIVGAGQAAFALAAKLRALKDERPITIIGSEDAYPYQRPPLSKkYLLGEMSFDRLMFRPEEWYAENNVDIRLTTFVEE 83
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSK-VLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 84 IDRAAKSVRMQDGSTLSYDKLVLATGAAPRELPASiGGDLEGVLTVRDKRDADRLFEEMKPGRRLLVIGGGYIGLEAAAV 163
Cdd:COG1251 82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIP-GADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 164 ARKLGLEVTLIEMADRILQRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGmDGRVAAAELSDGSVLDVDFVIVGIGVT 243
Cdd:COG1251 161 LRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 244 PNDRLARESGLDVGNGIVVDEHTRSSDKDIHAVGDCALlpWRGQL---VRLESVQNAVDQAEAAAHVLAGAEVAY-DAKP 319
Cdd:COG1251 240 PNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAE--HPGPVygrRVLELVAPAYEQARVAAANLAGGPAAYeGSVP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 320 WFWSDQYEVKLQIAGFNLGYDETVLRPGAREGSWSVWYFRDGRFVAVDAVNDAKAYVSGKKLLDTGAEPDRAILADPSAD 399
Cdd:COG1251 318 STKLKVFGVDVASAGDAEGDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALP 397
|
....
gi 1718777603 400 LKLL 403
Cdd:COG1251 398 LKEL 401
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
23-334 |
3.08e-102 |
|
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: 305.97 E-value: 3.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 23 ALKDERPITIIGSEDAYPYQRPPLSKKYLLGEMSFDRLMFRPEEWYAENNVDIRLTTFVEEIDRAAKSVRMQDGSTLSYD 102
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 103 KLVLATGAAPRELPasI-GGDLEGVLTVRDKRDADRLFEEMK--PGRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADR 179
Cdd:COG0446 81 KLVLATGARPRPPP--IpGLDLPGVFTLRTLDDADALREALKefKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 180 ILQRVaAKETADIMRGIHQEHGVSIREKTGLVRLVGmDGRVaAAELSDGSVLDVDFVIVGIGVTPNDRLARESGLDVG-- 257
Cdd:COG0446 159 LLGVL-DPEMAALLEEELREHGVELRLGETVVAIDG-DDKV-AVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGer 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718777603 258 NGIVVDEHTRSSDKDIHAVGDCALL--PWRGQLVRLESVQNAVDQAEAAAHVLAGAEVAYDAKPWFWSDQYEVKLQIAG 334
Cdd:COG0446 236 GWIKVDETLQTSDPDVYAAGDCAEVphPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFDLCIASTG 314
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
5-395 |
1.72e-81 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 255.24 E-value: 1.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 5 LVIVGAGQAAFALAAKLRALKDERPITIIGSEDAYPYQRPPLSKKYLLGEMSFDRLMFrPEEWYAENNVDIRLTTFVEEI 84
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVL-PANWWQENNVHLHSGVTIKTL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 85 DRAAKSVRMQDGSTLSYDKLVLATGAAPRELPA--SIGgdlEGVLTVRDKRDADRLFEEMKPGRRLLVIGGGYIGLEAAA 162
Cdd:PRK09754 85 GRDTRELVLTNGESWHWDQLFIATGAAARPLPLldALG---ERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 163 VARKLGLEVTLIEMADRILQRVAAKETADIMRGIHQEHGVSIREKTGLVRLVgmDGRVAAAELSDGSVLDVDFVIVGIGV 242
Cdd:PRK09754 162 SATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVV--DGEKVELTLQSGETLQADVVIYGIGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 243 TPNDRLARESGLDVGNGIVVDEHTRSSDKDIHAVGDCAL--LPwRGQLVRLESVQNAVDQAEAAAHVLAGAEVAYDAKPW 320
Cdd:PRK09754 240 SANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAItrLD-NGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPW 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718777603 321 FWSDQYEVKLQIAGfNLGYDETVLRpGAREGSWSVWY-FRDGRFVAVDAVNDAKAYVSGKKLLDTGAEPDRAILAD 395
Cdd:PRK09754 319 FWSDQYSDNLQFIG-DMRGDDWLCR-GNPETQKAIWFnLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLID 392
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
21-301 |
3.30e-62 |
|
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: 202.55 E-value: 3.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 21 LRALKDERPITIIGSEDAYPYQRPPLSKkYLLGEMSFDRLMFRPEEWYA---------ENNVDIRLTTFVEEIDRAAKSV 91
Cdd:pfam07992 17 LTLAQLGGKVTLIEDEGTCPYGGCVLSK-ALLGAAEAPEIASLWADLYKrkeevvkklNNGIEVLLGTEVVSIDPGAKKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 92 RMQ-----DGSTLSYDKLVLATGAAPRELPASiGGDLEGVLTVRDKRDADRLFEEMKPGRrLLVIGGGYIGLEAAAVARK 166
Cdd:pfam07992 96 VLEelvdgDGETITYDRLVIATGARPRLPPIP-GVELNVGFLVRTLDSAEALRLKLLPKR-VVVVGGGYIGVELAAALAK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 167 LGLEVTLIEMADRILqRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGmDGRVAAAELSDGSVLDVDFVIVGIGVTPND 246
Cdd:pfam07992 174 LGKEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIG-DGDGVEVILKDGTEIDADLVVVAIGRRPNT 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1718777603 247 RLARESGL--DVGNGIVVDEHTRSSDKDIHAVGDCallpwrgQLVRLESVQNAVDQA 301
Cdd:pfam07992 252 ELLEAAGLelDERGGIVVDEYLRTSVPGIYAAGDC-------RVGGPELAQNAVAQG 301
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
5-338 |
1.68e-55 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 195.43 E-value: 1.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 5 LVIVGAGQAAFALAAKLRAL-KDERPITIIGSEDAYPYQRPPLSKkYLLGEMSFDRLMFRPEEWYAENNVDIRLTTFVEE 83
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLnRHMFEITIFGEEPHPNYNRILLSS-VLQGEADLDDITLNSKDWYEKHGITLYTGETVIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 84 IDRAAKSVRMQDGSTLSYDKLVLATGAAPRELPASiGGDLEGVLTVRDKRDADRLFEEMKPGRRLLVIGGGYIGLEAAAV 163
Cdd:TIGR02374 80 IDTDQKQVITDAGRTLSYDKLILATGSYPFILPIP-GADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 164 ARKLGLEVTLIEMADRILQRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGmDGRVAAAELSDGSVLDVDFVIVGIGVT 243
Cdd:TIGR02374 159 LQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG-ATKADRIRFKDGSSLEADLIVMAAGIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 244 PNDRLARESGLDVGNGIVVDEHTRSSDKDIHAVGDCAllPWRGQLVRLesVQNAVDQAEAAA-HVLAGAEVAYDAkpwfw 322
Cdd:TIGR02374 238 PNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECA--EHNGRVYGL--VAPLYEQAKVLAdHICGVECEEYEG----- 308
|
330
....*....|....*.
gi 1718777603 323 SDqYEVKLQIAGFNLG 338
Cdd:TIGR02374 309 SD-LSAKLKLLGVDVW 323
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
4-280 |
5.50e-43 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 155.97 E-value: 5.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 4 RLVIVGAGQAAFALAAKLRALKDERPITIIGSEDAYPYQRPPLSkkYLLGEMsFD---RLMFRPEEWYAENNVDIRLTTF 80
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLP--YFVGGF-FDdpnTMIARTPEEFIKSGIDVKTEHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 81 VEEIDRAAKSVRMQDGSTLS-----YDKLVLATGAAPReLPASIGGDLEGVLTVRDKRDADRLFEEMKPGR--RLLVIGG 153
Cdd:PRK09564 79 VVKVDAKNKTITVKNLKTGSifndtYDKLMIATGARPI-IPPIKNINLENVYTLKSMEDGLALKELLKDEEikNIVIIGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 154 GYIGLEAAAVARKLGLEVTLIEMADRILQRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGmDGRVAAAELSDGSVlDV 233
Cdd:PRK09564 158 GFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIG-EDKVEGVVTDKGEY-EA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1718777603 234 DFVIVGIGVTPNDRLARESGLD-VGNG-IVVDEHTRSSDKDIHAVGDCA 280
Cdd:PRK09564 236 DVVIVATGVKPNTEFLEDTGLKtLKNGaIIVDEYGETSIENIYAAGDCA 284
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
21-312 |
4.39e-41 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 149.30 E-value: 4.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 21 LRALKDERPITIIGSEDAYPYQRPPLSKKYLLGEMSFDRLMFRPEEWYAENNVDIRLTTFVEEIDRAAKSVrMQDGSTLS 100
Cdd:PRK04965 21 IRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDLTRQSAGEFAEQFNLRLFPHTWVTDIDAEAQVV-KSQGNQWQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 101 YDKLVLATGAAPRELPasIGGDlEGVLTVRDKRDADRLFEEMKPGRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRI 180
Cdd:PRK04965 100 YDKLVLATGASAFVPP--IPGR-ELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 181 LQRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGMDGRVAAaELSDGSVLDVDFVIVGIGVTPNDRLARESGLDVGNGI 260
Cdd:PRK04965 177 LASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRA-TLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNRGI 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1718777603 261 VVDEHTRSSDKDIHAVGDCAllPWRGQLvrLESVQNAVDQAEAAAHVLAGAE 312
Cdd:PRK04965 256 VVDSYLQTSAPDIYALGDCA--EINGQV--LPFLQPIQLSAMALAKNLLGQN 303
|
|
| Reductase_C |
pfam14759 |
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ... |
320-401 |
4.62e-37 |
|
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: 129.61 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 320 WFWSDQYEVKLQIAGFNLGYDETVLRPGAREGSWSVWYFRDGRFVAVDAVNDAKAYVSGKKLLDTGAEPDRAILADPSAD 399
Cdd:pfam14759 1 WFWSDQYDLKLQIAGLPTGADEVVLRGDPEDGAFSVFYLRDGRLVAVDAVNRPRDFMAARRLIARGASVDPAALADPAVD 80
|
..
gi 1718777603 400 LK 401
Cdd:pfam14759 81 LK 82
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
22-309 |
1.68e-35 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 134.10 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 22 RALKDERPITIIGSEDAYPYQrpPLSKKYLLGEMSFDRLMFRPEEWYAENNVDIRLTTfVEEIDRAAKSVRMQDGSTLSY 101
Cdd:COG1252 22 KKLGGDAEVTLIDPNPYHLFQ--PLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGE-VTGIDPEARTVTLADGRTLSY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 102 DKLVLATGAAPRELPasIGGDLEGVLTVRDKRDADRL-------FEEMKPGRRL--LVIGGGYIGLEAAA----VARKLG 168
Cdd:COG1252 99 DYLVIATGSVTNFFG--IPGLAEHALPLKTLEDALALrerllaaFERAERRRLLtiVVVGGGPTGVELAGelaeLLRKLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 169 ---------LEVTLIEMADRILQRVAAKeTADIMRGIHQEHGVSIREKTGLVRLVgmDGRVaaaELSDGSVLDVDFVIVG 239
Cdd:COG1252 177 rypgidpdkVRITLVEAGPRILPGLGEK-LSEAAEKELEKRGVEVHTGTRVTEVD--ADGV---TLEDGEEIPADTVIWA 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718777603 240 IGVTPNDrLARESGLDV--GNGIVVDEHTRS-SDKDIHAVGDCALLPWRGQLVRLESVQNAVDQAEAAAHVLA 309
Cdd:COG1252 251 AGVKAPP-LLADLGLPTdrRGRVLVDPTLQVpGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIA 322
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
65-320 |
2.56e-34 |
|
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: 132.52 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 65 EEWYAENNVDI-----RLTtfveeidrAAKSVRMQDGSTLSYDKLVLATGAAPRELPAsIGGDLEGVLTvrdkrdADRLF 139
Cdd:COG1249 98 EELLKKNGVDVirgraRFV--------DPHTVEVTGGETLTADHIVIATGSRPRVPPI-PGLDEVRVLT------SDEAL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 140 EEMKPGRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRILqRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGMDGR 219
Cdd:COG1249 163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLL-PGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 220 VaAAELSDGS---VLDVDFVIVGIGVTPN-DRLARES-GLDVGN--GIVVDEHTRSSDKDIHAVGDCALLPWrgqlvrLE 292
Cdd:COG1249 242 V-TVTLEDGGgeeAVEADKVLVATGRRPNtDGLGLEAaGVELDErgGIKVDEYLRTSVPGIYAIGDVTGGPQ------LA 314
|
250 260 270
....*....|....*....|....*....|.
gi 1718777603 293 SVqnAVDQAEAAAHVLAGAEVA---YDAKPW 320
Cdd:COG1249 315 HV--ASAEGRVAAENILGKKPRpvdYRAIPS 343
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
4-315 |
2.80e-32 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 129.08 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 4 RLVIVGAGQAAFALAAKL--RALKDERPITIIGSEDAYPYQRPPLSKKYllGEMSFDRLMFRPEEWYAENNVDIRLTTFV 81
Cdd:PRK14989 5 RLAIIGNGMVGHRFIEDLldKADAANFDITVFCEEPRIAYDRVHLSSYF--SHHTAEELSLVREGFYEKHGIKVLVGERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 82 EEIDRAAKSVRMQDGSTLSYDKLVLATGAAPReLPASIGGDLEGVLTVRDKRDADRLFEEMKPGRRLLVIGGGYIGLEAA 161
Cdd:PRK14989 83 ITINRQEKVIHSSAGRTVFYDKLIMATGSYPW-IPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 162 AVARKLGLEVTLIEMADRILQRVAAKETADIMRGIHQEHGVSIREKTGLVRLV--GMDGRvAAAELSDGSVLDVDFVIVG 239
Cdd:PRK14989 162 GALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqeGVEAR-KTMRFADGSELEVDFIVFS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718777603 240 IGVTPNDRLARESGLDVG--NGIVVDEHTRSSDKDIHAVGDCAllPWRGQLVRLesVQNAVDQAEAAAHVLAGAEVAY 315
Cdd:PRK14989 241 TGIRPQDKLATQCGLAVAprGGIVINDSCQTSDPDIYAIGECA--SWNNRVFGL--VAPGYKMAQVAVDHLLGSENAF 314
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
88-279 |
9.94e-22 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 96.42 E-value: 9.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 88 AKSVRMqDGSTLSYDKLVLATGAAPReLPASIGGDLEGVLTVRDKRDADRLfeemkPgRRLLVIGGGYIGLEAAAVARKL 167
Cdd:PRK06370 122 PNTVRV-GGETLRAKRIFINTGARAA-IPPIPGLDEVGYLTNETIFSLDEL-----P-EHLVIIGGGYIGLEFAQMFRRF 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 168 GLEVTLIEMADRILQRvAAKETADIMRGIHQEHGVSIREKTGLVRLVGMDGRVAAAELSDG--SVLDVDFVIVGIGVTPN 245
Cdd:PRK06370 194 GSEVTVIERGPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCNGgaPEITGSHILVAVGRVPN 272
|
170 180 190
....*....|....*....|....*....|....*...
gi 1718777603 246 -DRLARESG---LDVGNGIVVDEHTRSSDKDIHAVGDC 279
Cdd:PRK06370 273 tDDLGLEAAgveTDARGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
95-315 |
1.04e-21 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 96.40 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 95 DGSTLSYDKLVLATGAAPRELPASIGGDLEGVLTVRDkrdadrLFEEMKPGRRLLVIGGGYIGLEAAAVARKLGLEVTLI 174
Cdd:PRK06292 125 NGERIEAKNIVIATGSRVPPIPGVWLILGDRLLTSDD------AFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 175 EMADRIL-------QRVAAKETADIMRgIHQEHGVSIREKTGlvrlvgmDGRVAAAELSDGSV-LDVDFVIVGIGVTPN- 245
Cdd:PRK06292 199 ERGDRILpledpevSKQAQKILSKEFK-IKLGAKVTSVEKSG-------DEKVEELEKGGKTEtIEADYVLVATGRRPNt 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718777603 246 DRLARESG---LDVGNGIVVDEHTRSSDKDIHAVGDCAllpwrGQLVRLESvqnAVDQAEAAAHVLAGAEVAY 315
Cdd:PRK06292 271 DGLGLENTgieLDERGRPVVDEHTQTSVPGIYAAGDVN-----GKPPLLHE---AADEGRIAAENAAGDVAGG 335
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
91-320 |
1.12e-21 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 96.53 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 91 VRMQDGSTLSYDKLVLATGAAPRELP-ASIGGDL----EGVLTvrdkrdadrlFEEMkPGRrLLVIGGGYIGLEAAAVAR 165
Cdd:PRK06327 136 VTGEDETVITAKHVIIATGSEPRHLPgVPFDNKIildnTGALN----------FTEV-PKK-LAVIGAGVIGLELGSVWR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 166 KLGLEVTLIEMADRILQRVA---AKETADIM--RGIHQEHGVSIREktglVRLVGMDGRVAAAElSDGS--VLDVDFVIV 238
Cdd:PRK06327 204 RLGAEVTILEALPAFLAAADeqvAKEAAKAFtkQGLDIHLGVKIGE----IKTGGKGVSVAYTD-ADGEaqTLEVDKLIV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 239 GIGVTPN--DRLARESGLDVG-NG-IVVDEHTRSSDKDIHAVGDCALLPWrgqlvrLESVqnAVDQAEAAAHVLAG--AE 312
Cdd:PRK06327 279 SIGRVPNtdGLGLEAVGLKLDeRGfIPVDDHCRTNVPNVYAIGDVVRGPM------LAHK--AEEEGVAVAERIAGqkGH 350
|
....*...
gi 1718777603 313 VAYDAKPW 320
Cdd:PRK06327 351 IDYNTIPW 358
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
90-278 |
1.55e-20 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 92.90 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 90 SVRMQDGS-TLSYDKLVLATGAAPRELPA-SIGGDlegvlTVRDKRDADRLfEEMkPgRRLLVIGGGYIGLEAAAVARKL 167
Cdd:PRK06416 123 RVMTEDGEqTYTAKNIILATGSRPRELPGiEIDGR-----VIWTSDEALNL-DEV-P-KSLVVIGGGYIGVEFASAYASL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 168 GLEVTLIEMADRILQrVAAKETADIMRGIHQEHGVSIREKTGLVRLVGMDGRVAAAELSDGSV--LDVDFVIVGIGVTPN 245
Cdd:PRK06416 195 GAEVTIVEALPRILP-GEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVTVTLEDGGKEetLEADYVLVAVGRRPN 273
|
170 180 190
....*....|....*....|....*....|....*.
gi 1718777603 246 -DRLARES-GLDVGNG-IVVDEHTRSSDKDIHAVGD 278
Cdd:PRK06416 274 tENLGLEElGVKTDRGfIEVDEQLRTNVPNIYAIGD 309
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
71-279 |
1.44e-19 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 90.22 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 71 NNVDIrLTTFVEEIDraAKSVRMqDGSTLSYDKLVLATGAAPReLPASIGGDLeGVltvrdkrDADRLFEEMKPGRRLLV 150
Cdd:PRK06116 106 NGVDL-IEGFARFVD--AHTVEV-NGERYTADHILIATGGRPS-IPDIPGAEY-GI-------TSDGFFALEELPKRVAV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 151 IGGGYIGLEAAAVARKLGLEVTLIEMADRILQRVaakeTADIMRGIHQE---HGVSIREKTGLVRLVGMDGRVAAAELSD 227
Cdd:PRK06116 173 VGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGF----DPDIRETLVEEmekKGIRLHTNAVPKAVEKNADGSLTLTLED 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1718777603 228 GSVLDVDFVIVGIGVTPN-DRLARESG---LDVGNGIVVDEHTRSSDKDIHAVGDC 279
Cdd:PRK06116 249 GETLTVDCLIWAIGREPNtDGLGLENAgvkLNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
4-278 |
2.43e-19 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 89.46 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 4 RLVIVGAGQAAFALAAKLRALKDERPITIIGSEDAYPYQRPPLSkkYLLGEMSFDR---LMFRPEEWYAENNVDIRLTTF 80
Cdd:PRK13512 3 KIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALP--YYIGEVVEDRkyaLAYTPEKFYDRKQITVKTYHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 81 VEEIDRAAKSVRMQDGST-----LSYDKLVLATGAAPRELPAsiggDLEGVLTVRDKRDADRL--FEEMKPGRRLLVIGG 153
Cdd:PRK13512 81 VIAINDERQTVTVLNRKTneqfeESYDKLILSPGASANSLGF----ESDITFTLRNLEDTDAIdqFIKANQVDKALVVGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 154 GYIGLEAAAVARKLGLEVTLIEMADRILQRVaakeTADIMRGIHQE---HGVSIREKTGLVRLVGmdgrvAAAELSDGSV 230
Cdd:PRK13512 157 GYISLEVLENLYERGLHPTLIHRSDKINKLM----DADMNQPILDEldkREIPYRLNEEIDAING-----NEVTFKSGKV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1718777603 231 LDVDFVIVGIGVTPNDRLARESG--LDVGNGIVVDEHTRSSDKDIHAVGD 278
Cdd:PRK13512 228 EHYDMIIEGVGTHPNSKFIESSNikLDDKGFIPVNDKFETNVPNIYAIGD 277
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
72-280 |
4.38e-19 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 87.10 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 72 NVDIRLTTfVEEIDRA--AKSVRMQDGSTLSYDKLVLATGAAPRELPasiggdLEGVLTVRDKR-----DADRLFeemKP 144
Cdd:COG0492 71 GAEILLEE-VTSVDKDdgPFRVTTDDGTEYEAKAVIIATGAGPRKLG------LPGEEEFEGRGvsycaTCDGFF---FR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 145 GRRLLVIGGGYIGLEAAAVARKLGLEVTLI-----EMADRILQ-RVAAKEtadimrgihqehGVSIREKTGLVRLVGmDG 218
Cdd:COG0492 141 GKDVVVVGGGDSALEEALYLTKFASKVTLIhrrdeLRASKILVeRLRANP------------KIEVLWNTEVTEIEG-DG 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718777603 219 RVAAAELSDG-----SVLDVDFVIVGIGVTPNDRLARESGLDV--GNGIVVDEHTRSSDKDIHAVGDCA 280
Cdd:COG0492 208 RVEGVTLKNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELdeDGYIVVDEDMETSVPGVFAAGDVR 276
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
65-278 |
1.65e-17 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 83.85 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 65 EEWYAENNVDIRL----TTFVeeidrAAKSVRMQDGSTLSYDKLVLATGAAPReLPASIGGDLEGVLTVRDKRDADRLfe 140
Cdd:PRK07846 94 EEYRGRDTPNIDVyrghARFI-----GPKTLRTGDGEEITADQVVIAAGSRPV-IPPVIADSGVRYHTSDTIMRLPEL-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 141 emkPgRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRILqRVAAKETADIMRGIHQEHgVSIREKTGLVRLVGMDGRV 220
Cdd:PRK07846 166 ---P-ESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLL-RHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSGV 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718777603 221 aAAELSDGSVLDVDFVIVGIGVTPN-DRL-ARESGLDVGNG--IVVDEHTRSSDKDIHAVGD 278
Cdd:PRK07846 240 -TLRLDDGSTVEADVLLVATGRVPNgDLLdAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGD 300
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
147-228 |
3.12e-17 |
|
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: 75.70 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 147 RLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRILqRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGmDGRVAAAELS 226
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEG-NGDGVVVVLT 78
|
..
gi 1718777603 227 DG 228
Cdd:pfam00070 79 DG 80
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
101-309 |
9.50e-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: 75.56 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 101 YDKLVLATGA-APRELPASiGGDLEGVLT----VRDKRDADRLFEEMKPGRRLLVIGGGYIGLEAAAVARKLG-LEVTLI 174
Cdd:COG0493 207 FDAVFLATGAgKPRDLGIP-GEDLKGVHSamdfLTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 175 EMADRilqrvaAKETADIMRgIH--QEHGVSIREKTGLVRLVGM-DGRVAAAELSD------------------GS--VL 231
Cdd:COG0493 286 YRRTR------EEMPASKEE-VEeaLEEGVEFLFLVAPVEIIGDeNGRVTGLECVRmelgepdesgrrrpvpieGSefTL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 232 DVDFVIVGIGVTPNDR-LARESGLDV-GNG-IVVDEHT-RSSDKDIHAVGDCAllpwRGQlvrlESVQNAVDQA-EAAAH 306
Cdd:COG0493 359 PADLVILAIGQTPDPSgLEEELGLELdKRGtIVVDEETyQTSLPGVFAGGDAV----RGP----SLVVWAIAEGrKAARA 430
|
...
gi 1718777603 307 VLA 309
Cdd:COG0493 431 IDR 433
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
42-278 |
2.02e-14 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 74.42 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 42 QRPPLSKKYLLGEMSFDRLMFRPEE-----------WYAENNVDIRLTT--FVeeiDRAAKSVRMQDGS--TLSYDKLVL 106
Cdd:PRK05249 67 QNPLYSSYRVKLRITFADLLARADHvinkqvevrrgQYERNRVDLIQGRarFV---DPHTVEVECPDGEveTLTADKIVI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 107 ATGAAPRElPASIGGDLEGVLtvrdkrDADRLFEEMKPGRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRILQrVAA 186
Cdd:PRK05249 144 ATGSRPYR-PPDVDFDHPRIY------DSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLS-FLD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 187 KETADIMRGIHQEHGVSIREKTGLVRLVG-MDGRVaaAELSDGSVLDVDFVIVGIGVTPN-DRLARES-GLDVGN-G-IV 261
Cdd:PRK05249 216 DEISDALSYHLRDSGVTIRHNEEVEKVEGgDDGVI--VHLKSGKKIKADCLLYANGRTGNtDGLNLENaGLEADSrGqLK 293
|
250
....*....|....*..
gi 1718777603 262 VDEHTRSSDKDIHAVGD 278
Cdd:PRK05249 294 VNENYQTAVPHIYAVGD 310
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
101-314 |
4.31e-13 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 70.59 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 101 YDKLVLATGA-APRELPASiGGDLEGVL-------TVRDKRDADRLFEemkpGRRLLVIGGGYIGLEAAAVARKLGLE-V 171
Cdd:PRK11749 226 YDAVFIGTGAgLPRFLGIP-GENLGGVYsavdfltRVNQAVADYDLPV----GKRVVVIGGGNTAMDAARTAKRLGAEsV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 172 TLI------EMADRILQRVAAKetadimrgihqEHGVSIREKTGLVRLVGMDGRVAAAEL-------SDGS--------- 229
Cdd:PRK11749 301 TIVyrrgreEMPASEEEVEHAK-----------EEGVEFEWLAAPVEILGDEGRVTGVEFvrmelgePDASgrrrvpieg 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 230 ---VLDVDFVIVGIGVTPNDRLARES-GLDV---GNGIVVDEHTRSSDKDIHAVGDCAllpwRGQ-LVrLESVQNAVDQA 301
Cdd:PRK11749 370 sefTLPADLVIKAIGQTPNPLILSTTpGLELnrwGTIIADDETGRTSLPGVFAGGDIV----TGAaTV-VWAVGDGKDAA 444
|
250
....*....|...
gi 1718777603 302 EAAAHVLAGAEVA 314
Cdd:PRK11749 445 EAIHEYLEGAASA 457
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
94-278 |
5.93e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 66.70 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 94 QDGSTLSYDKLVLATGAAPRELPasiggdLEGVLTVRDKRDADRLFEEMKPGRRLLVIGGGYIGLEAAAVARKLGLEVTL 173
Cdd:PRK07251 112 DEKIELTAETIVINTGAVSNVLP------IPGLADSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 174 IEMADRILQRVaAKETADIMRGIHQEHGVSIREKTGLVRLVGMDGRVAAAelSDGSVLDVDFVIVGIGVTPN-DRLARES 252
Cdd:PRK07251 186 LDAASTILPRE-EPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVV--TEDETYRFDALLYATGRKPNtEPLGLEN 262
|
170 180
....*....|....*....|....*....
gi 1718777603 253 ---GLDVGNGIVVDEHTRSSDKDIHAVGD 278
Cdd:PRK07251 263 tdiELTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
91-283 |
1.40e-11 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 65.65 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 91 VRMQDGS--TLSYDKLVLATGAAPRELPASIGgDLEGVLTVRDKRDADRLFEEmkpgrrLLVIGGGYIGLEAAAVARKLG 168
Cdd:PRK07845 128 VTTADGGeeTLDADVVLIATGASPRILPTAEP-DGERILTWRQLYDLDELPEH------LIVVGSGVTGAEFASAYTELG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 169 LEVTLIEMADRILQRVAAkETADIMRGIHQEHGVSI--REKTGLVRLVGmDGRVaaAELSDGSVLDVDFVIVGIGVTPND 246
Cdd:PRK07845 201 VKVTLVSSRDRVLPGEDA-DAAEVLEEVFARRGMTVlkRSRAESVERTG-DGVV--VTLTDGRTVEGSHALMAVGSVPNT 276
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1718777603 247 R---LArESGLDVGNG--IVVDEHTRSSDKDIHAVGDC-ALLP 283
Cdd:PRK07845 277 AglgLE-EAGVELTPSghITVDRVSRTSVPGIYAAGDCtGVLP 318
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
98-280 |
1.47e-11 |
|
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: 65.64 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 98 TLSYDKLVLATGAAPRELpaSIGGDLEGVLTvrdkrdADRLFEEMK-PGRRLlVIGGGYIGLEAAAVARKLGLEVTLieM 176
Cdd:TIGR01438 141 IYSAERFLIATGERPRYP--GIPGAKELCIT------SDDLFSLPYcPGKTL-VVGASYVALECAGFLAGIGLDVTV--M 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 177 ADRILQRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGMDGRVAA--AELSDGSVLDVDFVIVGIGVTPN-DRLARES- 252
Cdd:TIGR01438 210 VRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVefTDSTNGIEEEYDTVLLAIGRDACtRKLNLENv 289
|
170 180 190
....*....|....*....|....*....|.
gi 1718777603 253 GLDVG---NGIVVDEHTRSSDKDIHAVGDCA 280
Cdd:TIGR01438 290 GVKINkktGKIPADEEEQTNVPYIYAVGDIL 320
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
90-283 |
2.48e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 62.09 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 90 SVRMQDGST--LSYDKLVLATGAAPRELPasiggdLEGVLTVRDKRDADRLFEEMKPgRRLLVIGGGYIGLEAAAVARKL 167
Cdd:PRK13748 220 IVRLNDGGErvVAFDRCLIATGASPAVPP------IPGLKETPYWTSTEALVSDTIP-ERLAVIGSSVVALELAQAFARL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 168 GLEVTliemadrILQR--VAAKETADIMRGIH---QEHGVSIREKTGLVRLVGMDGR----VAAAELSdgsvldVDFVIV 238
Cdd:PRK13748 293 GSKVT-------ILARstLFFREDPAIGEAVTaafRAEGIEVLEHTQASQVAHVDGEfvltTGHGELR------ADKLLV 359
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1718777603 239 GIGVTPNDR-LARESG---LDVGNGIVVDEHTRSSDKDIHAVGDCALLP 283
Cdd:PRK13748 360 ATGRAPNTRsLALDAAgvtVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
100-283 |
2.87e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 61.16 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 100 SYDKLVLATGA-APRELPASiGGDLEGVLT-------VRDKRDADRLFEEMKP--GRRLLVIGGGYIGLEAAAVARKLGL 169
Cdd:PRK12770 118 KYDAVLIATGTwKSRKLGIP-GEDLPGVYSaleylfrIRAAKLGYLPWEKVPPveGKKVVVVGAGLTAVDAALEAVLLGA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 170 EVtlIEMADRILQRVAAKETADIMRGIhqEHGVSIREKTGLVRLVGmDGRVAAAELSD------------------GS-- 229
Cdd:PRK12770 197 EK--VYLAYRRTINEAPAGKYEIERLI--ARGVEFLELVTPVRIIG-EGRVEGVELAKmrlgepdesgrprpvpipGSef 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1718777603 230 VLDVDFVIVGIGVTPNDRLARES---GLDVGNGIVVDEHTRSSDKDIHAVGDCALLP 283
Cdd:PRK12770 272 VLEADTVVFAIGEIPTPPFAKEClgiELNRKGEIVVDEKHMTSREGVFAAGDVVTGP 328
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
92-280 |
1.02e-09 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 60.22 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 92 RMQDGSTLSYDKLVLATGAAPrELPASIGGDLEGVLTvrdkrdADRLFEEMKPGRRLLVIGGGYIGLEAAAVARKLGLEV 171
Cdd:PTZ00052 136 DNSQEETITAKYILIATGGRP-SIPEDVPGAKEYSIT------SDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 172 TLiemADR-ILQRVAAKETADIMRGIHQEHGVSIREKTGLVRLVGMDGRVaAAELSDGSVLDVDFVIVGIGVTPN-DRLA 249
Cdd:PTZ00052 209 TV---AVRsIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKI-KVLFSDGTTELFDTVLYATGRKPDiKGLN 284
|
170 180 190
....*....|....*....|....*....|....*
gi 1718777603 250 RES-GLDV---GNGIVVDEHTRSSdkDIHAVGDCA 280
Cdd:PTZ00052 285 LNAiGVHVnksNKIIAPNDCTNIP--NIFAVGDVV 317
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
72-278 |
1.79e-09 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 59.26 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 72 NVDIrLTTFVEEIDRAAKSVRMQDGS-TLSYDKLVLATGAAprelpaSIGGDLEGVLTVRDKRDADRLFEEMKPGRRLLV 150
Cdd:PRK08010 91 NIDV-IDGQAEFINNHSLRVHRPEGNlEIHGEKIFINTGAQ------TVVPPIPGITTTPGVYDSTGLLNLKELPGHLGI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 151 IGGGYIGLEAAAVARKLGLEVTLIEMADRILQRvAAKETADIMRGIHQEHGVSIREKTGLVRLVGMDGRVAAAelSDGSV 230
Cdd:PRK08010 164 LGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVH--SEHAQ 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1718777603 231 LDVDFVIVGIGVTPNDR--LARESGLDVGN--GIVVDEHTRSSDKDIHAVGD 278
Cdd:PRK08010 241 LAVDALLIASGRQPATAslHPENAGIAVNErgAIVVDKYLHTTADNIWAMGD 292
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
142-278 |
2.34e-09 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 59.37 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 142 MKPGRRLLVIGGGYIGLEAAAVARKLGLE-VTLI------EMADRILQRVAAKETADIMRGIHQEHGVSIREKTGL--VR 212
Cdd:PRK12778 567 IKFGKKVAVVGGGNTAMDSARTAKRLGAErVTIVyrrseeEMPARLEEVKHAKEEGIEFLTLHNPIEYLADEKGWVkqVV 646
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718777603 213 LVGMD-------GRVAAAELSDGSV-LDVDFVIVGIGVTPNDRLARE-SGLDVG--NGIVVDEHTRSSDKDIHAVGD 278
Cdd:PRK12778 647 LQKMElgepdasGRRRPVAIPGSTFtVDVDLVIVSVGVSPNPLVPSSiPGLELNrkGTIVVDEEMQSSIPGIYAGGD 723
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
82-291 |
2.43e-09 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 58.86 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 82 EEIDRAAKSVRMQDGSTLSYDKLVLATGAAPrELPasiggDLEGVLTVRDKRDadrlFEEMKPGRRLLVIGGGYIGLEAA 161
Cdd:PTZ00058 184 EVTIVSAGVSQLDDGQVIEGKNILIAVGNKP-IFP-----DVKGKEFTISSDD----FFKIKEAKRIGIAGSGYIAVELI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 162 AVARKLGLEVTLIEMADRILQRVAAKETADIMRGIhQEHGVSI-----------REKTGLVRLVGmDGRvaaAELSdgsv 230
Cdd:PTZ00058 254 NVVNRLGAESYIFARGNRLLRKFDETIINELENDM-KKNNINIithanveeiekVKEKNLTIYLS-DGR---KYEH---- 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718777603 231 ldVDFVIVGIGVTPNDRLARESGLDV---GNGIVVDEHTRSSDKDIHAVGDCALLPWRGQLVRL 291
Cdd:PTZ00058 325 --FDYVIYCVGRSPNTEDLNLKALNIktpKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEIEDL 386
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
98-278 |
4.37e-09 |
|
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: 58.06 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 98 TLSYDKLVLATGAAPRELpaSIGGDlEGVLTvrdkrdADRLFEEMKPGRRLLVIGGGYIGLEAAAV---ARKLGLEVTLI 174
Cdd:TIGR01423 149 RLQAEHILLATGSWPQML--GIPGI-EHCIS------SNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLC 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 175 EMADRILQRVAAKETADIMRGIhQEHGVSIR--EKTGLVRLvGMDGRvAAAELSDGSVLDVDFVIVGIGvtpndRLARES 252
Cdd:TIGR01423 220 YRNNMILRGFDSTLRKELTKQL-RANGINIMtnENPAKVTL-NADGS-KHVTFESGKTLDVDVVMMAIG-----RVPRTQ 291
|
170 180 190
....*....|....*....|....*....|....*
gi 1718777603 253 GLDVGN---------GIVVDEHTRSSDKDIHAVGD 278
Cdd:TIGR01423 292 TLQLDKvgveltkkgAIQVDEFSRTNVPNIYAIGD 326
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
91-278 |
4.75e-09 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 57.90 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 91 VRMQDGSTLSY--DKLVLATGAapRELPASIGGDLEGVLTvrdkrDADRLFEEMKpgRRLLVIGGGYIGLEAAAVARKLG 168
Cdd:PLN02507 156 VTQLDGTKLRYtaKHILIATGS--RAQRPNIPGKELAITS-----DEALSLEELP--KRAVVLGGGYIAVEFASIWRGMG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 169 LEVTLIEMADRILQRVAAKETADIMRGIhQEHGVSIREKTGLVRLVGMDGRVAAAeLSDGSVLDVDFVIVGIGVTPN-DR 247
Cdd:PLN02507 227 ATVDLFFRKELPLRGFDDEMRAVVARNL-EGRGINLHPRTNLTQLTKTEGGIKVI-TDHGEEFVADVVLFATGRAPNtKR 304
|
170 180 190
....*....|....*....|....*....|....
gi 1718777603 248 LARESG---LDVGNGIVVDEHTRSSDKDIHAVGD 278
Cdd:PLN02507 305 LNLEAVgveLDKAGAVKVDEYSRTNIPSIWAIGD 338
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
101-319 |
1.48e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 56.66 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 101 YDKLVLATGAAPRELPASIGGDLEGVLT----VRDKRDADRLfeemKPGRRLLVIGGGYIGLEAAAVARKLGLE-VTlie 175
Cdd:PRK12814 279 FDAVLLAVGAQKASKMGIPGEELPGVISgidfLRNVALGTAL----HPGKKVVVIGGGNTAIDAARTALRLGAEsVT--- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 176 madrILQRVAAKET----ADIMRGIHQehGVSIREKTGLVRLVGMDGR--VAAAELSDGS-----------------VLD 232
Cdd:PRK12814 352 ----ILYRRTREEMpanrAEIEEALAE--GVSLRELAAPVSIERSEGGleLTAIKMQQGEpdesgrrrpvpvegsefTLQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 233 VDFVIVGIGVTPNDRLARESGLDVG-NG-IVVDEHT-RSSDKDIHAVGDCALLPwrgqlvrlESVQNAVDQAEAAAHV-- 307
Cdd:PRK12814 426 ADTVISAIGQQVDPPIAEAAGIGTSrNGtVKVDPETlQTSVAGVFAGGDCVTGA--------DIAINAVEQGKRAAHAid 497
|
250
....*....|....
gi 1718777603 308 --LAGAEVAYDAKP 319
Cdd:PRK12814 498 lfLNGKPVTAPVQP 511
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
145-278 |
1.81e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 53.10 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 145 GRRLLVIGGGYIGLEAAAVARKLGLEVTLI------EMADRILQRVAAKetadimrgihqEHGVSIREKTGLVRLVG-MD 217
Cdd:PRK12831 281 GKKVAVVGGGNVAMDAARTALRLGAEVHIVyrrseeELPARVEEVHHAK-----------EEGVIFDLLTNPVEILGdEN 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 218 GRVAAAEL-------SDGS-------------VLDVDFVIVGIGVTPNDRLARES-GLDV-GNG-IVVDEHT-RSSDKDI 273
Cdd:PRK12831 350 GWVKGMKCikmelgePDASgrrrpveiegsefVLEVDTVIMSLGTSPNPLISSTTkGLKInKRGcIVADEETgLTSKEGV 429
|
....*
gi 1718777603 274 HAVGD 278
Cdd:PRK12831 430 FAGGD 434
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
98-282 |
5.09e-06 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 48.22 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 98 TLSYDKLVLATGAAPRELpaSIGGDLEGVLTVRDKRDA----DRLFE----------EMKPGRRLL---VIGGGYIGLEA 160
Cdd:PTZ00318 111 SVPYDKLVVAHGARPNTF--NIPGVEERAFFLKEVNHArgirKRIVQcieraslpttSVEERKRLLhfvVVGGGPTGVEF 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 161 AA--------VARKLGLE------VTLIEMADRILQRVAAKETADIMRGIHQEHgVSIREKTGLVRLvgMDGRVAaaeLS 226
Cdd:PTZ00318 189 AAeladffrdDVRNLNPElveeckVTVLEAGSEVLGSFDQALRKYGQRRLRRLG-VDIRTKTAVKEV--LDKEVV---LK 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1718777603 227 DGSVLDVDFVIVGIGVTPNDrLARESGLD-VGNG-IVVDEHTRSSD-KDIHAVGDCALL 282
Cdd:PTZ00318 263 DGEVIPTGLVVWSTGVGPGP-LTKQLKVDkTSRGrISVDDHLRVKPiPNVFALGDCAAN 320
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
101-280 |
1.20e-05 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 47.18 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 101 YDKLVLATGA-APRELPASiGGDLEGVLT-VRDKRDadrlFEEMKP---GRRLLVIGGGYIGLEAAAVARKLGL-EVTLI 174
Cdd:PRK12771 223 FDAVFVAIGAqLGKRLPIP-GEDAAGVLDaVDFLRA----VGEGEPpflGKRVVVIGGGNTAMDAARTARRLGAeEVTIV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 175 EMADRILQRVAAKETADIMRgihqeHGVSIREKTGLVRLVGMDGRVAAA--------ELSDGS----------VLDVDFV 236
Cdd:PRK12771 298 YRRTREDMPAHDEEIEEALR-----EGVEINWLRTPVEIEGDENGATGLrvitvekmELDEDGrpspvtgeeeTLEADLV 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1718777603 237 IVGIGVTPNDR-LARESGLDVGNGIV-VDEHTRSSDKD-IHAVGDCA 280
Cdd:PRK12771 373 VLAIGQDIDSAgLESVPGVEVGRGVVqVDPNFMMTGRPgVFAGGDMV 419
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
147-244 |
2.33e-04 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 43.31 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 147 RLLVIGGGYIGLEAAAVARKLGLEVTLIEMA-----------------------------------------------DR 179
Cdd:PRK07845 3 RIVIIGGGPGGYEAALVAAQLGADVTVIERDglggaavltdcvpsktliataevrtelrraaelgirfiddgearvdlPA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 180 ILQRV---AAKETADIMRGIhQEHGVSIREKTGLVRLVGMDGRVAAAELSDGS--VLDVDFVIVGIGVTP 244
Cdd:PRK07845 83 VNARVkalAAAQSADIRARL-EREGVRVIAGRGRLIDPGLGPHRVKVTTADGGeeTLDADVVLIATGASP 151
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
95-278 |
3.54e-04 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 42.56 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 95 DGSTLSYDKLVLATGAAPrELPasiggDLEGVLTVRDKRDADRLfeEMKPgRRLLVIGGGYIGLEAAAVARKLGLEVTLI 174
Cdd:PLN02546 211 DGKLYTARNILIAVGGRP-FIP-----DIPGIEHAIDSDAALDL--PSKP-EKIAIVGGGYIALEFAGIFNGLKSDVHVF 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 175 EMADRILqRVAAKETADI------MRGI--HQEHG--VSIREKTGLVRLvgmdgrvaaaELSDGSVLDVDFVIVGIGVTP 244
Cdd:PLN02546 282 IRQKKVL-RGFDEEVRDFvaeqmsLRGIefHTEESpqAIIKSADGSLSL----------KTNKGTVEGFSHVMFATGRKP 350
|
170 180 190
....*....|....*....|....*....|....*...
gi 1718777603 245 NDR-LARES---GLDVGNGIVVDEHTRSSDKDIHAVGD 278
Cdd:PLN02546 351 NTKnLGLEEvgvKMDKNGAIEVDEYSRTSVPSIWAVGD 388
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
142-241 |
1.10e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 40.38 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 142 MKPGRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRILQRvAAKETADimrgihqeHGVSIREKTGLVRLVGMDGRva 221
Cdd:cd05188 132 LKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLEL-AKELGAD--------HVIDYKEEDLEEELRLTGGG-- 200
|
90 100
....*....|....*....|
gi 1718777603 222 aaelsdgsvlDVDFVIVGIG 241
Cdd:cd05188 201 ----------GADVVIDAVG 210
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
150-180 |
1.33e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 37.13 E-value: 1.33e-03
10 20 30
....*....|....*....|....*....|.
gi 1718777603 150 VIGGGYIGLEAAAVARKLGLEVTLIEMADRI 180
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRL 31
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
146-185 |
1.71e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 40.26 E-value: 1.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1718777603 146 RRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRILQRVA 185
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKIL 40
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
147-180 |
2.80e-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: 39.30 E-value: 2.80e-03
10 20 30
....*....|....*....|....*....|....
gi 1718777603 147 RLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRI 180
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDP 34
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
147-191 |
2.86e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 38.63 E-value: 2.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1718777603 147 RLLVIGGGYIGLEAAAVARKLGLEVTLIEMadrilqRVAAKETAD 191
Cdd:pfam01262 30 KVLVIGGGVAGLNAAATAKGLGAIVTILDV------RPARLEQLE 68
|
|
| Zn_ADH7 |
cd08261 |
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ... |
143-209 |
3.61e-03 |
|
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176222 [Multi-domain] Cd Length: 337 Bit Score: 39.09 E-value: 3.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718777603 143 KPGRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRILQRVAAKETADIMRGIHQEHGVSIREKTG 209
Cdd:cd08261 158 TAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTD 224
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
147-195 |
4.23e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 37.49 E-value: 4.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1718777603 147 RLLVIGGGYIGLEAAAVARKLGLEVTLIEMadrilqRVAAKETADIMRG 195
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDV------RPARLRQLESLLG 64
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
142-178 |
4.88e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 38.70 E-value: 4.88e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1718777603 142 MKPGRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMAD 178
Cdd:PRK06847 1 MAAVKKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDP 37
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
142-237 |
6.41e-03 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 38.22 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718777603 142 MKPGRRLLVIGGGYIGLEAAAVARKLGLEVTLIEMADRILQRvaAKETADIMRGIHQEHGVSIRektgLVRLVGMDGRVA 221
Cdd:PRK06130 1 MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALER--ARGVIERALGVYAPLGIASA----GMGRIRMEAGLA 74
|
90
....*....|....*.
gi 1718777603 222 AAelsdgsVLDVDFVI 237
Cdd:PRK06130 75 AA------VSGADLVI 84
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
148-175 |
7.55e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 38.52 E-value: 7.55e-03
10 20
....*....|....*....|....*...
gi 1718777603 148 LLVIGGGYIGLEAAAVARKLGLEVTLIE 175
Cdd:PRK12842 12 VLVIGSGAGGLSAAITARKLGLDVVVLE 39
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
148-175 |
7.79e-03 |
|
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: 38.14 E-value: 7.79e-03
10 20
....*....|....*....|....*...
gi 1718777603 148 LLVIGGGYIGLEAAAVARKLGLEVTLIE 175
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVE 33
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
149-184 |
9.54e-03 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 38.13 E-value: 9.54e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1718777603 149 LVIGGGYIGLEAAAVARKLGLEVTLIEMADRILQRV 184
Cdd:PLN02268 4 IVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRV 39
|
|
| |
