|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
3-394 |
2.98e-128 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 375.25 E-value: 2.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 3 KNFVIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPLLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISFFINTKVVK 82
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 83 INTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWSI 162
Cdd:COG1251 82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 163 LKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPN 242
Cdd:COG1251 162 RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 243 TKLVHDTAIKLNRGIVVDEKMRTNIDSVYAAGDVAEVNNEIEG-----LWGTALEQGRVAGSNMVSKTAIYKKEIPTTIF 317
Cdd:COG1251 242 TELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGrrvleLVAPAYEQARVAAANLAGGPAAYEGSVPSTKL 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489350042 318 NAFNVSLFSIGVVNKEqcDTTIVEED-GKEKYTRLFIKDNKIVGVISLEGVAASIPYKSAIEKHVSLEGIDLLNTNIS 394
Cdd:COG1251 322 KVFGVDVASAGDAEGD--EEVVVRGDpARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALP 397
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
6-379 |
4.37e-72 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 240.50 E-value: 4.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 6 VIIGSGVAAVNAAKTIREYDKGS-NIFIFGEEPLLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISFFINTKVVKIN 84
Cdd:TIGR02374 2 VLVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 85 TDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWSILK 164
Cdd:TIGR02374 82 TDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 165 AGKKVSIVEVAPLLMRRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPNTK 244
Cdd:TIGR02374 162 LGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 245 LVHDTAIKLNRGIVVDEKMRTNIDSVYAAGDVAEVNNEIEGLWGTALEQGRVAGSNMV-SKTAIYKKEIPTTIFNAFNVS 323
Cdd:TIGR02374 242 LAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICgVECEEYEGSDLSAKLKLLGVD 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489350042 324 LFSIGVVNK-EQCDTTIVEEDGKEKYTRLFIKDNKIVGVI------------SLEGVAASIPYKSAIEK 379
Cdd:TIGR02374 322 VWSAGDAQEtERTTSIKIYDEQKGIYKKLVLSDDKLLGAVlfgdtsdygrllDMVLKQADISEDPAIIK 390
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
25-328 |
1.38e-69 |
|
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: 221.99 E-value: 1.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 25 DKGSNIFIFGEEPLLPYKRIKLSKDLYSDLHS-EKVLIKKKKWYQDNHISFFINTKVVKINTDEQFIVTSNEAVFSYHKL 103
Cdd:COG0446 3 GPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDpEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYDKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 104 LICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKE--SVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLLMRR 181
Cdd:COG0446 83 VLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKgkRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 182 qLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTgIKMNDNSQINCDSIVYSIGVTPNTKLVHDTAIKLNR--GIVV 259
Cdd:COG0446 163 -LDPEMAALLEEELREHGVELRLGETVVAIDGDDKVA-VTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgWIKV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489350042 260 DEKMRTNIDSVYAAGDVAEVNNEIEG------LWGTALEQGRVAGSNMVSKTAIYkKEIPTTIFNAFNVSLFSIG 328
Cdd:COG0446 241 DETLQTSDPDVYAAGDCAEVPHPVTGktvyipLASAANKQGRVAAENILGGPAPF-PGLGTFISKVFDLCIASTG 314
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
6-294 |
3.25e-55 |
|
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: 184.44 E-value: 3.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 6 VIIGSGVAAVNAAKTIREYdkGSNIFIFGEEPLLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQD---------NHISFFI 76
Cdd:pfam07992 4 VVIGGGPAGLAAALTLAQL--GGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKRkeevvkklnNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 77 NTKVVKINTDEQFI-----VTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKgHLEDKESVVTIGG 151
Cdd:pfam07992 82 GTEVVSIDPGAKKVvleelVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALR-LKLLPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 152 GVQGLETAWSILKAGKKVSIVEVAPLLMRrQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCD 231
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDAD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489350042 232 SIVYSIGVTPNTKLVHDTAIKLNR--GIVVDEKMRTNIDSVYAAGDVAEVnneIEGLWGTALEQG 294
Cdd:pfam07992 240 LVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDCRVG---GPELAQNAVAQG 301
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
2-302 |
1.13e-46 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 164.71 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 2 EKNFVIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPLLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISFFINTKVV 81
Cdd:PRK09754 3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 82 KINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWS 161
Cdd:PRK09754 83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 162 ILKAGKKVSIVEVAPLLMRRQLDTK-SSLLLKRKIEKeGVKVYLNTSIDSILGKESVTgIKMNDNSQINCDSIVYSIGVT 240
Cdd:PRK09754 163 ATQRRCKVTVIELAATVMGRNAPPPvQRYLLQRHQQA-GVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVVIYGIGIS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489350042 241 PNTKLVHDTAIKLNRGIVVDEKMRTNIDSVYAAGDVA---EVNNEIE--GLWGTALEQGRVAGSNMV 302
Cdd:PRK09754 241 ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAitrLDNGALHrcESWENANNQAQIAAAAML 307
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
6-355 |
3.03e-45 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 161.75 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 6 VIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPL-------LPYkrikLSKDLYSDlhSEKVLIKKKKWYQDNHISFFINT 78
Cdd:PRK09564 4 IIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIvsfgacgLPY----FVGGFFDD--PNTMIARTPEEFIKSGIDVKTEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 79 KVVKINTDEQFIVTSN---EAVF--SYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKE--SVVTIGG 151
Cdd:PRK09564 78 EVVKVDAKNKTITVKNlktGSIFndTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEikNIVIIGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 152 GVQGLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKmNDNSQINCD 231
Cdd:PRK09564 158 GFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVV-TDKGEYEAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 232 SIVYSIGVTPNTKLVHDTAIKL--NRGIVVDEKMRTNIDSVYAAGDVAEVNNEIEG------LWGTALEQGRVAGSNMVS 303
Cdd:PRK09564 237 VVIVATGVKPNTEFLEDTGLKTlkNGAIIVDEYGETSIENIYAAGDCATIYNIVSNknvyvpLATTANKLGRMVGENLAG 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489350042 304 KtaiyKKEIPTTIFNAfnvslfSIGVVNKEQCDTTIVEEDGKE---KYTRLFIKD 355
Cdd:PRK09564 317 R----HVSFKGTLGSA------CIKVLDLEAARTGLTEEEAKKlgiDYKTVFIKD 361
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
6-357 |
1.12e-36 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 142.18 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 6 VIIGSGVAAvnaAKTIREY-DKGS----NIFIFGEEPLLPYKRIKLSKdLYSDLHSEKVLIKKKKWYQDNHISFFINTKV 80
Cdd:PRK14989 7 AIIGNGMVG---HRFIEDLlDKADaanfDITVFCEEPRIAYDRVHLSS-YFSHHTAEELSLVREGFYEKHGIKVLVGERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 81 VKINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAW 160
Cdd:PRK14989 83 ITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 161 SILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSIL--GKESVTGIKMNDNSQINCDSIVYSIG 238
Cdd:PRK14989 163 ALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqeGVEARKTMRFADGSELEVDFIVFSTG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 239 VTPNTKLVHDTAIKLNR--GIVVDEKMRTNIDSVYAAGDVAEVNNEIEGLWGTALEQGRVAGSNMVSKTAIYKKEIPTTI 316
Cdd:PRK14989 243 IRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGSENAFEGADLSAK 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489350042 317 FNAFNVSLFSIGVVN--KEQCDTTIVEEDGKEKYTRLFI-KDNK 357
Cdd:PRK14989 323 LKLLGVDVGGIGDAHgrTPGARSYVYLDESKEIYKRLIVsEDNK 366
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
1-280 |
1.76e-36 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 136.59 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 1 MEKNFVIIGSGVAAVNAAKTIREYDKGSNIFIF----GEEpllpYKRIKLSKdLYSDLHSEKVLIKKK--KWYQDNHISF 74
Cdd:PRK04965 1 MSNGIVIIGSGFAARQLVKNIRKQDAHIPITLItadsGDE----YNKPDLSH-VFSQGQRADDLTRQSagEFAEQFNLRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKINTDEQfIVTSNEAVFSYHKLLICTGANNRRLEINGinKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQ 154
Cdd:PRK04965 76 FPHTWVTDIDAEAQ-VVKSQGNQWQYDKLVLATGASAFVPPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 155 GLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIV 234
Cdd:PRK04965 153 GTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489350042 235 YSIGVTPNTKLVHDTAIKLNRGIVVDEKMRTNIDSVYAAGDVAEVN 280
Cdd:PRK04965 233 AAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEIN 278
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
90-317 |
6.94e-30 |
|
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: 119.81 E-value: 6.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 90 IVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLedkesVVtIGGGVQGLETAwSILKA-GKK 168
Cdd:COG1249 121 VEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEALELEELPKSL-----VV-IGGGYIGLEFA-QIFARlGSE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 169 VSIVEVAPLLMRRqLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNS---QINCDSIVYSIGVTPNTKL 245
Cdd:COG1249 194 VTLVERGDRLLPG-EDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGGgeeAVEADKVLVATGRRPNTDG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 246 VH-DTA-IKLNR--GIVVDEKMRTNIDSVYAAGDVAevnneieglwG------TALEQGRVAGSNMV---SKTAIYKKeI 312
Cdd:COG1249 273 LGlEAAgVELDErgGIKVDEYLRTSVPGIYAIGDVT----------GgpqlahVASAEGRVAAENILgkkPRPVDYRA-I 341
|
....*
gi 489350042 313 PTTIF 317
Cdd:COG1249 342 PSVVF 346
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
75-277 |
9.87e-29 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 114.06 E-value: 9.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKIN-TDEQFIV-TSNEAVFSYHKLLICTGANNRRLEINGInkkniftirdmkeaDELKGH------------L 140
Cdd:COG0492 74 ILLEEVTSVDkDDGPFRVtTDDGTEYEAKAVIIATGAGPRKLGLPGE--------------EEFEGRgvsycatcdgffF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 141 EDKEsVVTIGGGVQGLETAWSILKAGKKVSIVevapllMRRQlDTKSSLLLKRKIEK-EGVKVYLNTSIDSILGKESVTG 219
Cdd:COG0492 140 RGKD-VVVVGGGDSALEEALYLTKFASKVTLI------HRRD-ELRASKILVERLRAnPKIEVLWNTEVTEIEGDGRVEG 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489350042 220 IKMNDN-----SQINCDSIVYSIGVTPNTKLVHDTAIKLNRG--IVVDEKMRTNIDSVYAAGDVA 277
Cdd:COG0492 212 VTLKNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVR 276
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
6-300 |
4.85e-24 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 102.52 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 6 VIIGSGVAAVNAAKTIREYDKG---------SNIFIFGeePLLPY---KRIKLSKDLYsDLhsEKVLikkkkwyQDNHIS 73
Cdd:COG1252 5 VIVGGGFAGLEAARRLRKKLGGdaevtlidpNPYHLFQ--PLLPEvaaGTLSPDDIAI-PL--RELL-------RRAGVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 74 FfINTKVVKINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGInKKNIFTIRDMKEADELKGHLED---------KE 144
Cdd:COG1252 73 F-IQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGL-AEHALPLKTLEDALALRERLLAaferaerrrLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 145 SVVTIGGGVQGLETA------------WSILKAGK-KVSIVEVAPLLMRRqLDTKSSLLLKRKIEKEGVKVYLNTSIDSI 211
Cdd:COG1252 151 TIVVVGGGPTGVELAgelaellrkllrYPGIDPDKvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTEV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 212 LGkesvTGIKMNDNSQINCDSIVYSIGVTPNtKLVHDTAIKLNRG--IVVDEKMRT-NIDSVYAAGDVAEVNNEIEGLWG 288
Cdd:COG1252 230 DA----DGVTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCAAVPDPDGKPVP 304
|
330
....*....|....*.
gi 489350042 289 ----TALEQGRVAGSN 300
Cdd:COG1252 305 ktaqAAVQQAKVLAKN 320
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
75-317 |
6.39e-22 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 96.94 E-value: 6.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKINTdeqfivTSNEAVFSYHKLLICTGANNRrlEINGINKKNIFTIRDMKEADELKghlEDKESVVTIGGGVQ 154
Cdd:TIGR01350 113 FLDPGTVSVTG------ENGEETLEAKNIIIATGSRPR--SLPGPFDFDGKVVITSTGALNLE---EVPESLVIIGGGVI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 155 GLETAWSILKAGKKVSIVEVAPLLMRrQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQ--INCDS 232
Cdd:TIGR01350 182 GIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGETetLTGEK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 233 IVYSIGVTPNTKL--VHDTAIKLN-RG-IVVDEKMRTNIDSVYAAGDVaevnneIEG--LWGTALEQGRVAGSNMV--SK 304
Cdd:TIGR01350 261 VLVAVGRKPNTEGlgLEKLGVELDeRGrIVVDEYMRTNVPGIYAIGDV------IGGpmLAHVASHEGIVAAENIAgkEP 334
|
250
....*....|...
gi 489350042 305 TAIYKKEIPTTIF 317
Cdd:TIGR01350 335 AHIDYDAVPSVIY 347
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
75-276 |
1.04e-21 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 94.23 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKI-NTDEQFIV-TSNEAVFSYHKLLICTGANNRRLEINGINKkniFTIRDMKEADELKGHL-EDKEsVVTIGG 151
Cdd:TIGR01292 73 IIYEEVIKVdKSDRPFKVyTGDGKEYTAKAVIIATGASARKLGIPGEDE---FWGRGVSYCATCDGPFfKNKE-VAVVGG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 152 GVQGLETAWSILKAGKKVSIVEvapllmRRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDN-----S 226
Cdd:TIGR01292 149 GDSAIEEALYLTRIAKKVTLVH------RRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDNKVEGVKIKNTvtgeeE 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489350042 227 QINCDSIVYSIGVTPNTKLVHDtAIKLNRG--IVVDEKMRTNIDSVYAAGDV 276
Cdd:TIGR01292 223 ELEVDGVFIAIGHEPNTELLKG-LLELDENgyIVTDEGMRTSVPGVFAAGDV 273
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
75-317 |
1.18e-21 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 96.40 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKINtdEQFIVTSNeavfsyhkLLICTGAnnRRLEING---INKKNIFTIRDMKEADELKghledkESVVTIGG 151
Cdd:PRK06292 116 FVDPNTVEVN--GERIEAKN--------IVIATGS--RVPPIPGvwlILGDRLLTSDDAFELDKLP------KSLAVIGG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 152 GVQGLETA--WSILkaGKKVSIVEVAPLLMRRQlDTKSSLLLKRKIEKEgVKVYLNTSIDSI--LGKESVTGIKMNDNSQ 227
Cdd:PRK06292 178 GVIGLELGqaLSRL--GVKVTVFERGDRILPLE-DPEVSKQAQKILSKE-FKIKLGAKVTSVekSGDEKVEELEKGGKTE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 228 -INCDSIVYSIGVTPNTKLVH--DTAIKL-NRG-IVVDEKMRTNIDSVYAAGDvaeVNNEIEgLWGTALEQGRVAGSNMV 302
Cdd:PRK06292 254 tIEADYVLVATGRRPNTDGLGleNTGIELdERGrPVVDEHTQTSVPGIYAAGD---VNGKPP-LLHEAADEGRIAAENAA 329
|
250
....*....|....*..
gi 489350042 303 SKTAIY--KKEIPTTIF 317
Cdd:PRK06292 330 GDVAGGvrYHPIPSVVF 346
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
6-347 |
1.61e-19 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 89.84 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 6 VIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPLLPYKRIKLSKDLYSDLHSEK--VLIKKKKWYQDNHISFFINTKVVKI 83
Cdd:PRK13512 5 IVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKyaLAYTPEKFYDRKQITVKTYHEVIAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 84 NTDEQFIVTSN---EAVF--SYHKLLICTGANNRRLeinGINKKNIFTIRDMKEADELKGHLE--DKESVVTIGGGVQGL 156
Cdd:PRK13512 85 NDERQTVTVLNrktNEQFeeSYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIDQFIKanQVDKALVVGAGYISL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 157 ETAWSILKAGKKVSIVEVAPLLMRrQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKEsvtgIKMNDNSQINCDSIVYS 236
Cdd:PRK13512 162 EVLENLYERGLHPTLIHRSDKINK-LMDADMNQPILDELDKREIPYRLNEEIDAINGNE----VTFKSGKVEHYDMIIEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 237 IGVTPNTKLVHDTAIKLNRG--IVVDEKMRTNIDSVYAAGDVAE-------VNNEIEGLWGTALEQGRVAGSNMVSKTAI 307
Cdd:PRK13512 237 VGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIITshyrhvdLPASVPLAWGAHRAASIVAEQIAGNDTIE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489350042 308 YKKEIPTTIFNAFNVSLFSIGVVNKE--QCDTTIVEEDGKEK 347
Cdd:PRK13512 317 FKGFLGNNIVKFFDYTFASVGVKPNElkQFDYKMVEVTQGAH 358
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
91-276 |
4.91e-19 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 88.72 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 91 VTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLedkesvVTIGGGVQGLETAWSILKAGKKVS 170
Cdd:PRK06370 125 VRVGGETLRAKRIFINTGARAAIPPIPGLDEVGYLTNETIFSLDELPEHL------VIIGGGYIGLEFAQMFRRFGSEVT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 171 IVEVAPLLMRRQlDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMN---DNSQINCDSIVYSIGVTPNT-KLV 246
Cdd:PRK06370 199 VIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDcngGAPEITGSHILVAVGRVPNTdDLG 277
|
170 180 190
....*....|....*....|....*....|...
gi 489350042 247 HDTA-IKLNR--GIVVDEKMRTNIDSVYAAGDV 276
Cdd:PRK06370 278 LEAAgVETDArgYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
103-277 |
1.99e-18 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 86.74 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 103 LLICTGANNRrlEINGIN--KKNIFTIRDMKEADELKghledkESVVTIGGGVQGLE--TAWSILkaGKKVSIVEVAPLL 178
Cdd:PRK06416 138 IILATGSRPR--ELPGIEidGRVIWTSDEALNLDEVP------KSLVVIGGGYIGVEfaSAYASL--GAEVTIVEALPRI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 179 MRRQlDTKSSLLLKRKIEKEGVKVYLNTSIDSIlgKESVTGIKMND-----NSQINCDSIVYSIGVTPNTKLV--HDTAI 251
Cdd:PRK06416 208 LPGE-DKEISKLAERALKKRGIKIKTGAKAKKV--EQTDDGVTVTLedggkEETLEADYVLVAVGRRPNTENLglEELGV 284
|
170 180
....*....|....*....|....*..
gi 489350042 252 KLNRG-IVVDEKMRTNIDSVYAAGDVA 277
Cdd:PRK06416 285 KTDRGfIEVDEQLRTNVPNIYAIGDIV 311
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
6-317 |
2.24e-18 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 86.36 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 6 VIIGSGV----AAVNAA---------------------------KTIREydKGSNIFIFGEEPLlpYKRIKLSKDL-YSD 53
Cdd:PRK05249 9 VVIGSGPagegAAMQAAklgkrvavieryrnvgggcthtgtipsKALRE--AVLRLIGFNQNPL--YSSYRVKLRItFAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 54 L--HSEKVLIK----KKKWYQDNHISFFI--------NTKVVKINTDEQFIVTSNeavfsyhKLLICTGANNRRLEINGI 119
Cdd:PRK05249 85 LlaRADHVINKqvevRRGQYERNRVDLIQgrarfvdpHTVEVECPDGEVETLTAD-------KIVIATGSRPYRPPDVDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 120 NKKNIF---TIRDMKEadelkghleDKESVVTIGGGVQGLETAwSILKA-GKKVSIVEvapllmRRQ-----LDTKSSLL 190
Cdd:PRK05249 158 DHPRIYdsdSILSLDH---------LPRSLIIYGAGVIGCEYA-SIFAAlGVKVTLIN------TRDrllsfLDDEISDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 191 LKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPNTKLVHDTAIKL---NRG-IVVDEKMRTN 266
Cdd:PRK05249 222 LSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNTDGLNLENAGLeadSRGqLKVNENYQTA 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489350042 267 IDSVYAAGDVaevnneI--EGLWGTALEQGRVAGSNMV-SKTAIYKKEIPTTIF 317
Cdd:PRK05249 302 VPHIYAVGDV------IgfPSLASASMDQGRIAAQHAVgEATAHLIEDIPTGIY 349
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
75-361 |
5.59e-17 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 82.47 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKINtdeqfivtSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKghledkESVVTIGGGVQ 154
Cdd:TIGR02053 112 FKDPKTVKVD--------LGREVRGAKRFLIATGARPAIPPIPGLKEAGYLTSEEALALDRIP------ESLAVIGGGAI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 155 GLETAWSILKAGKKVSIVEVAPLLMRRQlDTKSSLLLKRKIEKEGVKVYLNTSIDSI---LGKESVTGIKMNDNSQINCD 231
Cdd:TIGR02053 178 GVELAQAFARLGSEVTILQRSDRLLPRE-EPEISAAVEEALAEEGIEVVTSAQVKAVsvrGGGKIITVEKPGGQGEVEAD 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 232 SIVYSIGVTPNTKLVH--DTAIKLNR--GIVVDEKMRTNIDSVYAAGDVAEvNNEIEGLwgtALEQGRVAGSNMV--SKT 305
Cdd:TIGR02053 257 ELLVATGRRPNTDGLGleKAGVKLDErgGILVDETLRTSNPGIYAAGDVTG-GLQLEYV---AAKEGVVAAENALggANA 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489350042 306 AIYKKEIPTTIFNAFNVSlfSIGVVNKE------QCDTTIVEEDGKEK-----YTRLFIKDN------KIVGV 361
Cdd:TIGR02053 333 KLDLLVIPRVVFTDPAVA--SVGLTEAEaqkagiECDCRTLPLTNVPRarinrDTRGFIKLVaepgtgKVLGV 403
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
75-333 |
8.47e-15 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 75.56 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKINTDEQFIVTSNEAVfsyhklLICTGANNRRLEINGI-NKKNIFTIRDMKEADELKGHLEdkesvvTIGGGV 153
Cdd:PRK07251 100 FVSNKVIEVQAGDEKIELTAETI------VINTGAVSNVLPIPGLaDSKHVYDSTGIQSLETLPERLG------IIGGGN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 154 QGLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSLLlKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQInCDSI 233
Cdd:PRK07251 168 IGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALA-KQYMEEDGITFLLNAHTTEVKNDGDQVLVVTEDETYR-FDAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 234 VYSIGVTPNTKLVH--DTAIKLN-RG-IVVDEKMRTNIDSVYAAGDvaeVNNEIEGLWgTALEQGRVAGSNMV---SKTA 306
Cdd:PRK07251 246 LYATGRKPNTEPLGleNTDIELTeRGaIKVDDYCQTSVPGVFAVGD---VNGGPQFTY-ISLDDFRIVFGYLTgdgSYTL 321
|
250 260
....*....|....*....|....*..
gi 489350042 307 IYKKEIPTTIFnaFNVSLFSIGVVNKE 333
Cdd:PRK07251 322 EDRGNVPTTMF--ITPPLSQVGLTEKE 346
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
72-297 |
4.39e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 70.02 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 72 ISFFINTKVV------KINTDE--QFIVTSNEAVFSYHKLLICTGA-NNRRLEINGINKKNI-------FTIRDMKeade 135
Cdd:PRK12770 83 VVFHTRTKVCcgeplhEEEGDEfvERIVSLEELVKKYDAVLIATGTwKSRKLGIPGEDLPGVysaleylFRIRAAK---- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 136 lKGHLeDKES--------VVTIGGGVQGLETAWSILKAGkkvsiVEVAPLLMRRQLD----TKSSLllkRKIEKEGVKVY 203
Cdd:PRK12770 159 -LGYL-PWEKvppvegkkVVVVGAGLTAVDAALEAVLLG-----AEKVYLAYRRTINeapaGKYEI---ERLIARGVEFL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 204 LNTSIDSILGKESVTGIKM--------------------NDNSQINCDSIVYSIGVTPNTKL-VHDTAIKLNRG--IVVD 260
Cdd:PRK12770 229 ELVTPVRIIGEGRVEGVELakmrlgepdesgrprpvpipGSEFVLEADTVVFAIGEIPTPPFaKECLGIELNRKgeIVVD 308
|
250 260 270
....*....|....*....|....*....|....*..
gi 489350042 261 EKMRTNIDSVYAAGDVAEVNNEIeglwGTALEQGRVA 297
Cdd:PRK12770 309 EKHMTSREGVFAAGDVVTGPSKI----GKAIKSGLRA 341
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
75-281 |
4.75e-13 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 70.18 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKINTDEQFI----------VTSNEAVFSYHKLLICTGANNRRLEINGInKKNIFTIRDMKEADELKGHL---- 140
Cdd:PTZ00318 79 YLRAVVYDVDFEEKRVkcgvvsksnnANVNTFSVPYDKLVVAHGARPNTFNIPGV-EERAFFLKEVNHARGIRKRIvqci 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 141 ----------EDKE---SVVTIGGGVQGLETAWSI--------------LKAGKKVSIVEVAPLLMRrQLDTKSSLLLKR 193
Cdd:PTZ00318 158 eraslpttsvEERKrllHFVVVGGGPTGVEFAAELadffrddvrnlnpeLVEECKVTVLEAGSEVLG-SFDQALRKYGQR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 194 KIEKEGVKVYLNTSIDSILGKESVTgikmNDNSQINCDSIVYSIGVTPNTKLVHDTAIKLNRG-IVVDEKMRT-NIDSVY 271
Cdd:PTZ00318 237 RLRRLGVDIRTKTAVKEVLDKEVVL----KDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGrISVDDHLRVkPIPNVF 312
|
250
....*....|
gi 489350042 272 AAGDVAEVNN 281
Cdd:PTZ00318 313 ALGDCAANEE 322
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
75-276 |
1.36e-12 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 68.89 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 75 FINTKVVKINTDEQFIVTSNEAVFsyhkllICTGANNRRLEINGINKK-NIFTIRDMKEADELKGHLEdkesvvTIGGGV 153
Cdd:PRK08010 101 FINNHSLRVHRPEGNLEIHGEKIF------INTGAQTVVPPIPGITTTpGVYDSTGLLNLKELPGHLG------ILGGGY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 154 QGLETAWSILKAGKKVSIVEVAPLLMRRQlDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKmNDNSQINCDSI 233
Cdd:PRK08010 169 IGVEFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVH-SEHAQLAVDAL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489350042 234 VYSIGVTPNTKLVH--DTAIKLNR--GIVVDEKMRTNIDSVYAAGDV 276
Cdd:PRK08010 247 LIASGRQPATASLHpeNAGIAVNErgAIVVDKYLHTTADNIWAMGDV 293
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
60-317 |
3.42e-12 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 67.64 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 60 LIKKkkwyqdNHISFFINTKVVKINTDEQFIV----TSNEAVFSYHkLLICTGANNRRLEINGINKKNIFTIRDMKEADE 135
Cdd:PRK06327 109 LFKK------NKITVLKGRGSFVGKTDAGYEIkvtgEDETVITAKH-VIIATGSEPRHLPGVPFDNKIILDNTGALNFTE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 136 LKGHLedkesvVTIGGGVQGLETA--WSILkaGKKVSIVEVAPLLMRRQLDTKSSLLLKrKIEKEGVKVYLNTSIDSI-L 212
Cdd:PRK06327 182 VPKKL------AVIGAGVIGLELGsvWRRL--GAEVTILEALPAFLAAADEQVAKEAAK-AFTKQGLDIHLGVKIGEIkT 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 213 GKESVTgIKMND---NSQ-INCDSIVYSIGVTPNTK-LVHDTA-IKLN-RG-IVVDEKMRTNIDSVYAAGDVaevnneIE 284
Cdd:PRK06327 253 GGKGVS-VAYTDadgEAQtLEVDKLIVSIGRVPNTDgLGLEAVgLKLDeRGfIPVDDHCRTNVPNVYAIGDV------VR 325
|
250 260 270
....*....|....*....|....*....|....*.
gi 489350042 285 G--LWGTALEQGRVAGSNMVSKTA-IYKKEIPTTIF 317
Cdd:PRK06327 326 GpmLAHKAEEEGVAVAERIAGQKGhIDYNTIPWVIY 361
|
|
| Rubredoxin_C |
pfam18267 |
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin ... |
313-379 |
1.21e-11 |
|
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin oxidoreductase present in Clostridium acetobutylicum. The majority of obligatory anaerobes detoxify micro-aerobic environments by consuming O2 via H2O-forming NADH oxidase. This enzyme offers an alternate reaction pathway for scavenging of O2 and reactive oxygen species, wherein the reducing equivalent is obtained from NADH.
Pssm-ID: 408082 [Multi-domain] Cd Length: 70 Bit Score: 59.88 E-value: 1.21e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489350042 313 PTTIFNAFNVSLFSIGVVNK-EQCDTTIVEEDGKEKYTRLFIKDNKIVGVISLEGVAASIPYKSAIEK 379
Cdd:pfam18267 1 PSTILKVFGIDLFSMGDIEEnDNAEEIVKVDASNGIYKKLFIRDGKLVGAILIGDTSESPKLKKAIEK 68
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
102-354 |
1.45e-11 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 65.56 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 102 KLLICTGANNRRLEINGINkkniFTIrDMKEADELKghlEDKESVVTIGGGVQGLETAwSILKA-GKKVSivevapLLMR 180
Cdd:PRK06116 134 HILIATGGRPSIPDIPGAE----YGI-TSDGFFALE---ELPKRVAVVGAGYIAVEFA-GVLNGlGSETH------LFVR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 181 RQL-----DTKSSLLLKRKIEKEGVKVYLNTSIDSI--LGKESVTgIKMNDNSQINCDSIVYSIGVTPNTKLV--HDTAI 251
Cdd:PRK06116 199 GDAplrgfDPDIRETLVEEMEKKGIRLHTNAVPKAVekNADGSLT-LTLEDGETLTVDCLIWAIGREPNTDGLglENAGV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 252 KLN-RG-IVVDEKMRTNIDSVYAAGDvaeVNNEIEgLWGTALEQGRVagsnmVSKTAIYKKE--------IPTTIFnafn 321
Cdd:PRK06116 278 KLNeKGyIIVDEYQNTNVPGIYAVGD---VTGRVE-LTPVAIAAGRR-----LSERLFNNKPdekldysnIPTVVF---- 344
|
250 260 270
....*....|....*....|....*....|...
gi 489350042 322 vSLFSIGVVNkeqcdttIVEEDGKEKYTRLFIK 354
Cdd:PRK06116 345 -SHPPIGTVG-------LTEEEAREQYGEDNVK 369
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
146-279 |
4.94e-11 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 64.02 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 146 VVTIGGGVQGLETAwsILKAG--KKVSIVEVAPLLmrrqldtKSSLLLKRKIEK-EGVKVYLNTSIDSILGKES-VTGIK 221
Cdd:PRK15317 354 VAVIGGGNSGVEAA--IDLAGivKHVTVLEFAPEL-------KADQVLQDKLRSlPNVTIITNAQTTEVTGDGDkVTGLT 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489350042 222 MNDNS-----QINCDSIVYSIGVTPNTKLVHDTaIKLN-RG-IVVDEKMRTNIDSVYAAGDVAEV 279
Cdd:PRK15317 425 YKDRTtgeehHLELEGVFVQIGLVPNTEWLKGT-VELNrRGeIIVDARGATSVPGVFAAGDCTTV 488
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
145-224 |
7.58e-11 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 57.98 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 145 SVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLLMrRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMND 224
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
72-277 |
9.57e-11 |
|
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: 63.23 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 72 ISFFINTKVVK-INTDE---QFivtsnEAVFsyhkllICTGA-NNRRLEINGINKKNIFT----IRDMKEADELKGHLED 142
Cdd:COG0493 186 VEFRTNVEVGKdITLDElleEF-----DAVF------LATGAgKPRDLGIPGEDLKGVHSamdfLTAVNLGEAPDTILAV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 143 KESVVTIGGGVQGLETAWSILKAG-KKVSIVEvapllMRRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKES--VTG 219
Cdd:COG0493 255 GKRVVVIGGGNTAMDCARTALRLGaESVTIVY-----RRTREEMPASKEEVEEALEEGVEFLFLVAPVEIIGDENgrVTG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 220 IKM-------NDNS-------------QINCDSIVYSIGVTPNTKLVHDTA-IKLNRG--IVVDEK-MRTNIDSVYAAGD 275
Cdd:COG0493 330 LECvrmelgePDESgrrrpvpiegsefTLPADLVILAIGQTPDPSGLEEELgLELDKRgtIVVDEEtYQTSLPGVFAGGD 409
|
..
gi 489350042 276 VA 277
Cdd:COG0493 410 AV 411
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
95-275 |
1.10e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 63.25 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 95 EAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLedkesvVTIGGGVQGLETAWSILKAGKKVSIVEV 174
Cdd:PRK13748 228 ERVVAFDRCLIATGASPAVPPIPGLKETPYWTSTEALVSDTIPERL------AVIGSSVVALELAQAFARLGSKVTILAR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 175 APLLMRRqlDTKSSLLLKRKIEKEGVKVYLNTSIDSI--LGKESV--TGikmndNSQINCDSIVYSIGVTPNT-KLVHDT 249
Cdd:PRK13748 302 STLFFRE--DPAIGEAVTAAFRAEGIEVLEHTQASQVahVDGEFVltTG-----HGELRADKLLVATGRAPNTrSLALDA 374
|
170 180
....*....|....*....|....*....
gi 489350042 250 A-IKLN-RG-IVVDEKMRTNIDSVYAAGD 275
Cdd:PRK13748 375 AgVTVNaQGaIVIDQGMRTSVPHIYAAGD 403
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
96-277 |
7.26e-10 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 60.58 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 96 AVFsyhkllICTGANN-RRLEINGINKKNIF-------TIRDMKEADEL-KGhledkESVVTIGGGvqglETAW-----S 161
Cdd:PRK11749 228 AVF------IGTGAGLpRFLGIPGENLGGVYsavdfltRVNQAVADYDLpVG-----KRVVVIGGG----NTAMdaartA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 162 ILKAGKKVSIVevapllMRRQLD--TKSslllKRKIE---KEGVKVYLNTSIDSILGKE----SVTGIKMNDNSQ----- 227
Cdd:PRK11749 293 KRLGAESVTIV------YRRGREemPAS----EEEVEhakEEGVEFEWLAAPVEILGDEgrvtGVEFVRMELGEPdasgr 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489350042 228 -----------INCDSIVYSIGVTPNTKLVHDT-AIKLNR--GIVVDEK-MRTNIDSVYAAGDVA 277
Cdd:PRK11749 363 rrvpiegseftLPADLVIKAIGQTPNPLILSTTpGLELNRwgTIIADDEtGRTSLPGVFAGGDIV 427
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
144-276 |
7.53e-10 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 60.35 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 144 ESVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKrkIEKEGVKVYLNTSIDSILGKESVTGIKMN 223
Cdd:PRK07846 167 ESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTE--LASKRWDVRLGRNVVGVSQDGSGVTLRLD 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489350042 224 DNSQINCDSIVYSIGVTPNTKL--VHDTAIKLNRG--IVVDEKMRTNIDSVYAAGDV 276
Cdd:PRK07846 245 DGSTVEADVLLVATGRVPNGDLldAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGDV 301
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
79-276 |
3.14e-09 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 58.67 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 79 KVVKINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGinkKNIFTIRDmkEADELKghlEDKESVVTIGGGVQGLET 158
Cdd:PLN02507 147 KIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPNIPG---KELAITSD--EALSLE---ELPKRAVVLGGGYIAVEF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 159 AwSILKA-GKKVSIVEVAPLLMRrQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSI 237
Cdd:PLN02507 219 A-SIWRGmGATVDLFFRKELPLR-GFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFAT 296
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489350042 238 GVTPNTKLVH--DTAIKLNR--GIVVDEKMRTNIDSVYAAGDV 276
Cdd:PLN02507 297 GRAPNTKRLNleAVGVELDKagAVKVDEYSRTNIPSIWAIGDV 339
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
58-317 |
2.01e-08 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 56.01 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 58 KVLIKKKKWYQDNHISFFINTKVVKiNTDEQfivtSNEAVFSYHKLLICTGANNRRLEINGINKKNIftirdmkEADELK 137
Cdd:TIGR01438 107 RVALREKKVKYENAYAEFVDKHRIK-ATNKK----GKEKIYSAERFLIATGERPRYPGIPGAKELCI-------TSDDLF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 138 GHLEDKESVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLLmrRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKESV 217
Cdd:TIGR01438 175 SLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILL--RGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 218 TGIKMNDNSQINC---DSIVYSIGVTPNTKLVH--DTAIKLNRG---IVVDEKMRTNIDSVYAAGDVAEVNNEIEGLwgt 289
Cdd:TIGR01438 253 VLVEFTDSTNGIEeeyDTVLLAIGRDACTRKLNleNVGVKINKKtgkIPADEEEQTNVPYIYAVGDILEDKPELTPV--- 329
|
250 260 270
....*....|....*....|....*....|
gi 489350042 290 ALEQGRVAGSNMV--SKTAIYKKEIPTTIF 317
Cdd:TIGR01438 330 AIQAGRLLAQRLFkgSTVICDYENVPTTVF 359
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
70-274 |
2.40e-08 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 54.92 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 70 NHISFFINTKVVKIN-TDEQFIVTSNEAVFSYHKLLICTG--ANNRRLEINGINKKNiftiRDMKEADELKGhledkESV 146
Cdd:pfam13738 88 FELPINLFEEVTSVKkEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVPELPKHY----SYVKDFHPYAG-----QKV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 147 VTIGGGVQGLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSL------LLKRKIEKEGVKVYLNTSIDSILGKESVTGI 220
Cdd:pfam13738 159 VVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSLspdtlnRLEELVKNGKIKAHFNAEVKEITEVDVSYKV 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489350042 221 KMNDNSQINCDSI-VYSIGVTPNTKLVHDTAIKLNR-GIVV--DEKMRTNIDSVYAAG 274
Cdd:pfam13738 239 HTEDGRKVTSNDDpILATGYHPDLSFLKKGLFELDEdGRPVltEETESTNVPGLFLAG 296
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
104-297 |
9.86e-07 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 50.63 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 104 LICTGANNRRL---EINGinkKNIFTIRDMKEADELKGHLedkesvVTIGGGVQGLETAWSILKAGKKVSIV----EVAP 176
Cdd:PRK07845 144 LIATGASPRILptaEPDG---ERILTWRQLYDLDELPEHL------IVVGSGVTGAEFASAYTELGVKVTLVssrdRVLP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 177 llmrrQLDTKSSLLLKRKIEKEGVKVYLNTSIDSIlgkeSVTG----IKMNDNSQINCDSIVYSIGVTPNTK-LVHDTA- 250
Cdd:PRK07845 215 -----GEDADAAEVLEEVFARRGMTVLKRSRAESV----ERTGdgvvVTLTDGRTVEGSHALMAVGSVPNTAgLGLEEAg 285
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489350042 251 IKLNRG--IVVDEKMRTNIDSVYAAGDVAEVNneieGLWGTALEQGRVA 297
Cdd:PRK07845 286 VELTPSghITVDRVSRTSVPGIYAAGDCTGVL----PLASVAAMQGRIA 330
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
76-275 |
5.95e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 48.09 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 76 INTKVV---KINTDEQFIVTSNEAVFsyhkllICTGANNRR-LEINGINKKNIFTirdmkeADE-------LKGHLEDKE 144
Cdd:PRK12831 208 IETNVVvgkTVTIDELLEEEGFDAVF------IGSGAGLPKfMGIPGENLNGVFS------ANEfltrvnlMKAYKPEYD 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 145 S-------VVTIGGGVQGLETAWSILKAGKKVSIVevapllMRRqldTKSSLLLKRK----IEKEGVKVYLNTSIDSILG 213
Cdd:PRK12831 276 TpikvgkkVAVVGGGNVAMDAARTALRLGAEVHIV------YRR---SEEELPARVEevhhAKEEGVIFDLLTNPVEILG 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 214 KES--VTG---IKMN----DNS-------------QINCDSIVYSIGVTPNtKLVHDTA--IKLNRG--IVVDEKM-RTN 266
Cdd:PRK12831 347 DENgwVKGmkcIKMElgepDASgrrrpveiegsefVLEVDTVIMSLGTSPN-PLISSTTkgLKINKRgcIVADEETgLTS 425
|
....*....
gi 489350042 267 IDSVYAAGD 275
Cdd:PRK12831 426 KEGVFAGGD 434
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
117-276 |
7.19e-06 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 48.20 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 117 NGINKKNIFTIRD--MKEADEL-KGHLEDKESVVTIGGGVQGLETAWSILKAGkkvsiVEVAPLLMRRQLDTKSSLLLKR 193
Cdd:PRK12778 541 NGVMSSNEYLTRVnlMDAASPDsDTPIKFGKKVAVVGGGNTAMDSARTAKRLG-----AERVTIVYRRSEEEMPARLEEV 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 194 K-IEKEGVKVYLNTSIDSILGKE-----SVTGIKMN----DNS-------------QINCDSIVYSIGVTPNtKLVHDT- 249
Cdd:PRK12778 616 KhAKEEGIEFLTLHNPIEYLADEkgwvkQVVLQKMElgepDASgrrrpvaipgstfTVDVDLVIVSVGVSPN-PLVPSSi 694
|
170 180 190
....*....|....*....|....*....|
gi 489350042 250 -AIKLNR--GIVVDEKMRTNIDSVYAAGDV 276
Cdd:PRK12778 695 pGLELNRkgTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
149-317 |
3.02e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 45.97 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 149 IGGGVQGLETAWSILKAGKKVSI-VEVAPLlmrRQLDTKSSLLLKRKIEKEGVKvYLNTSIDSILGK-ESVTGIKMNDNS 226
Cdd:PTZ00052 188 VGASYIGLETAGFLNELGFDVTVaVRSIPL---RGFDRQCSEKVVEYMKEQGTL-FLEGVVPINIEKmDDKIKVLFSDGT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 227 QINCDSIVYSIGVTPNTKLVHDTAIKL-----NRGIVVDEKmrTNIDSVYAAGDVAEVNNEiegLWGTALEQGRVAGSNM 301
Cdd:PTZ00052 264 TELFDTVLYATGRKPDIKGLNLNAIGVhvnksNKIIAPNDC--TNIPNIFAVGDVVEGRPE---LTPVAIKAGILLARRL 338
|
170
....*....|....*...
gi 489350042 302 V--SKTAIYKKEIPTTIF 317
Cdd:PTZ00052 339 FkqSNEFIDYTFIPTTIF 356
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
140-286 |
5.28e-05 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 45.38 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 140 LEDKESVVTIGGGVQGLETAwSILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSILGKES--V 217
Cdd:PTZ00058 234 IKEAKRIGIAGSGYIAVELI-NVVNRLGAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEknL 312
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489350042 218 TGIKMNDNSQINCDSIVYSIGVTPNTKLVHDTAI--KLNRG-IVVDEKMRTNIDSVYAAGDVAEV--NNEIEGL 286
Cdd:PTZ00058 313 TIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALniKTPKGyIKVDDNQRTSVKHIYAVGDCCMVkkNQEIEDL 386
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
145-241 |
8.99e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.47 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 145 SVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLL--MRRQLDTK------SSLLLKRKIEK----EGVKVYLNTSIDSIL 212
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELggRAAQLHKTfpgldcPQCILEPLIAEveanPNITVYTGAEVEEVS 221
|
90 100 110
....*....|....*....|....*....|....
gi 489350042 213 GKE---SVTgIKMNDNS--QINCDSIVYSIGVTP 241
Cdd:COG1148 222 GYVgnfTVT-IKKGPREeiEIEVGAIVLATGFKP 254
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
141-278 |
9.91e-05 |
|
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: 44.19 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 141 EDKESVVTIGGGVQGLETAwSILKA----GKKVSIVEVAPLLMRrQLDTKSSLLLKRKIEKEGVKVYLNTSIDSI-LGKE 215
Cdd:TIGR01423 185 EPPRRVLTVGGGFISVEFA-GIFNAykprGGKVTLCYRNNMILR-GFDSTLRKELTKQLRANGINIMTNENPAKVtLNAD 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489350042 216 SVTGIKMNDNSQINCDSIVYSIGVTPNTKLVH--DTAIKL--NRGIVVDEKMRTNIDSVYAAGDVAE 278
Cdd:TIGR01423 263 GSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVELtkKGAIQVDEFSRTNVPNIYAIGDVTD 329
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
144-278 |
2.94e-04 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 42.94 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489350042 144 ESVVTIGGGVQGLETA--WSILKAGKKVSIVEVAPLlmrRQLDTKSSLLLKRKIEKEGVKVYLNTSIDSIL-GKESVTGI 220
Cdd:PLN02546 253 EKIAIVGGGYIALEFAgiFNGLKSDVHVFIRQKKVL---RGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIkSADGSLSL 329
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489350042 221 KMNDNSQINCDSIVYSIGVTPNTKLV--HDTAIKLNR--GIVVDEKMRTNIDSVYAAGDVAE 278
Cdd:PLN02546 330 KTNKGTVEGFSHVMFATGRKPNTKNLglEEVGVKMDKngAIEVDEYSRTSVPSIWAVGDVTD 391
|
|
|