|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
16-329 |
1.42e-93 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 281.24 E-value: 1.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 16 DLTIIGGGPTGIFAAFQCGMNNISCRIIESMsQLGGQLAALypeKHIYDVAGFPE-VPAIDLVESLWAQAERYNPDVVLG 94
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGG-EPGGQLATT---KEIENYPGFPEgISGPELAERLREQAERFGAEILLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 95 EAVTkyTKLDDGTFETRTNAGNVYRSRAVLIAAGLGafePRKLPqLGNIDHLTGSSVYYAVKS-VDNFKGKRVVIVGGGD 173
Cdd:COG0492 78 EVTS--VDKDDGPFRVTTDDGTEYEAKAVIIATGAG---PRKLG-LPGEEEFEGRGVSYCATCdGFFFRGKDVVVVGGGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 174 SALDWTVGLLKNAESVTLVHRAKEFQGHgktAHEVEQAKADGLIDVHLQTEVASIeESNGALTHVHLRSS-NGEEWTVEA 252
Cdd:COG0492 152 SALEEALYLTKFASKVTLIHRRDELRAS---KILVERLRANPKIEVLWNTEVTEI-EGDGRVEGVTLKNVkTGEEKELEV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501494460 253 DRLLILIGFKSNLGPLAGWDLELAEN-ALVVDSHMKTSVDGLYAAGDIAHYpgKLKIIQTGLSEATMAVRHSLSYIKP 329
Cdd:COG0492 228 DGVFVAIGLKPNTELLKGLGLELDEDgYIVVDEDMETSVPGVFAAGDVRDY--KYRQAATAAGEGAIAALSAARYLEP 303
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
16-299 |
4.24e-41 |
|
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: 145.85 E-value: 4.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 16 DLTIIGGGPTGIFAAFQCGMNNISCRIIESMsQLGGQLAAlypEKHIYDVAGFPE-VPAIDLVESLWAQAERYNPDVVLg 94
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGM-EPGGQLTT---TTEVENYPGFPEgISGPELMEKMKEQAVKFGAEIIY- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 95 EAVTKYTKLDDgTFETRTNAGNVYRSRAVLIAAGLgafEPRKLPQLGNiDHLTGSSVYY-AVKSVDNFKGKRVVIVGGGD 173
Cdd:TIGR01292 76 EEVIKVDKSDR-PFKVYTGDGKEYTAKAVIIATGA---SARKLGIPGE-DEFWGRGVSYcATCDGPFFKNKEVAVVGGGD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 174 SALDWTVGLLKNAESVTLVHRAKEFQGhgkTAHEVEQAKADGLIDVHLQTEVASIEESNGaLTHVHLRSS-NGEEWTVEA 252
Cdd:TIGR01292 151 SAIEEALYLTRIAKKVTLVHRRDKFRA---EKILLDRLKKNPKIEFLWNSTVEEIVGDNK-VEGVKIKNTvTGEEEELEV 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501494460 253 DRLLILIGFKSNLGPLAGwDLELAENA-LVVDSHMKTSVDGLYAAGDI 299
Cdd:TIGR01292 227 DGVFIAIGHEPNTELLKG-LLELDENGyIVTDEGMRTSVPGVFAAGDV 273
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
84-297 |
1.11e-26 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 107.31 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 84 AERYNPDVVLGEAVTKYTKLDDGtFETRTNAGnVYRSRAVLIAAGLGAFePRKLPQLGNIDHltgssvYYAVKSVDNFKG 163
Cdd:pfam13738 85 ADHFELPINLFEEVTSVKKEDDG-FVVTTSKG-TYQARYVIIATGEFDF-PNKLGVPELPKH------YSYVKDFHPYAG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 164 KRVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEFQGHGK---------TAHEVEQAKADGLIDVHLQTEVASIEESNGA 234
Cdd:pfam13738 156 QKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSdpsyslspdTLNRLEELVKNGKIKAHFNAEVKEITEVDVS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501494460 235 lthVHLRSSNGEEWTVEaDRLLILIGFKSNLGPLAGWDLELAENAL-VVDSH-MKTSVDGLYAAG 297
Cdd:pfam13738 236 ---YKVHTEDGRKVTSN-DDPILATGYHPDLSFLKKGLFELDEDGRpVLTEEtESTNVPGLFLAG 296
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
19-300 |
7.84e-25 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 104.49 E-value: 7.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLaalypekhIYDVAGFPEVPAIDL--VESLWAQAERYNPDVVLGEA 96
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLL--------RYGIPEFRLPKDIVDreVERLLKLGVEIRTNTEVGRD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 97 VTkytkLDDgTFEtrtnagnvyRSRAVLIAAGLGAfePRKLP----QLGN----IDHLTGSSVyyAVKSVDNFKGKRVVI 168
Cdd:PRK11749 217 IT----LDE-LRA---------GYDAVFIGTGAGL--PRFLGipgeNLGGvysaVDFLTRVNQ--AVADYDLPVGKRVVV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 169 VGGGDSALDWTVGLLKN-AESVTLVHR--AKEFQGhgkTAHEVEQAKADGLIDVHLQTEVASIEESNG--ALTHVHLRSS 243
Cdd:PRK11749 279 IGGGNTAMDAARTAKRLgAESVTIVYRrgREEMPA---SEEEVEHAKEEGVEFEWLAAPVEILGDEGRvtGVEFVRMELG 355
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501494460 244 N------------GEEWTVEADRLLILIGFKSNLGPLAGW-DLELAE--NALVVDSHMKTSVDGLYAAGDIA 300
Cdd:PRK11749 356 EpdasgrrrvpieGSEFTLPADLVIKAIGQTPNPLILSTTpGLELNRwgTIIADDETGRTSLPGVFAGGDIV 427
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
19-303 |
4.75e-23 |
|
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: 99.44 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLAalY--PE----KHIydvagfpevpaidlveslwAQAERynpDVV 92
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLR--YgiPEfrlpKDV-------------------LDREI---ELI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 93 LGEAVTkytklddgtFETRTNAGNVY-----RSR--AVLIAAGLGAfePRKLP----QLGNI----DHLTGSSVYYAVKS 157
Cdd:COG0493 182 EALGVE---------FRTNVEVGKDItldelLEEfdAVFLATGAGK--PRDLGipgeDLKGVhsamDFLTAVNLGEAPDT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 158 VDnFKGKRVVIVGGGDSALDwTVGLLK--NAESVTLVHR--AKEFQGHgktAHEVEQAKADGlIDVHLQTEVASIE-ESN 232
Cdd:COG0493 251 IL-AVGKRVVVIGGGNTAMD-CARTALrlGAESVTIVYRrtREEMPAS---KEEVEEALEEG-VEFLFLVAPVEIIgDEN 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 233 GALTHVHLR----------------SSNGEEWTVEADRLLILIGFKSNLGPLAG-WDLELAENALVV--DSHMKTSVDGL 293
Cdd:COG0493 325 GRVTGLECVrmelgepdesgrrrpvPIEGSEFTLPADLVILAIGQTPDPSGLEEeLGLELDKRGTIVvdEETYQTSLPGV 404
|
330
....*....|
gi 501494460 294 YAAGDIAHYP 303
Cdd:COG0493 405 FAGGDAVRGP 414
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
16-316 |
3.28e-20 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 89.30 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 16 DLTIIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLAALYPEkhIYDVAGFPEVPAI--DLVESLWAQAERYNPDV-- 91
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPYGGCVLSKA--LLGAAEAPEIASLwaDLYKRKEEVVKKLNNGIev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 92 VLGEAVTKYTKlDDGTF---ETRTNAGNVYRSRAVLIAAGlgaFEPRKLP----QLGNIDHLTGSSVYYAVKSVDnfKGK 164
Cdd:pfam07992 80 LLGTEVVSIDP-GAKKVvleELVDGDGETITYDRLVIATG---ARPRLPPipgvELNVGFLVRTLDSAEALRLKL--LPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 165 RVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEF-QGHGKTAHEVEQA--KADGlIDVHLQTEVASIEESNGALThVHLr 241
Cdd:pfam07992 154 RVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLlRAFDEEISAALEKalEKNG-VEVRLGTSVKEIIGDGDGVE-VIL- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501494460 242 sSNGEEwtVEADRLLILIGFKSNLGPLAGWDLELAE-NALVVDSHMKTSVDGLYAAGDIAHypGKLKIIQTGLSEA 316
Cdd:pfam07992 231 -KDGTE--IDADLVVVAIGRRPNTELLEAAGLELDErGGIVVDEYLRTSVPGIYAAGDCRV--GGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
16-322 |
3.06e-18 |
|
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: 85.52 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 16 DLTIIGGGPTGIFAAFQCGMNNISCRIIESmSQLGG--------------QLAALYpeKHIYDVAGF---PEVPAID--- 75
Cdd:COG1249 5 DLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGtclnvgcipskallHAAEVA--HEARHAAEFgisAGAPSVDwaa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 76 -----------LVESLWAQAERYNPDVVLGEAvtkyTKLDDGTFETrtNAGNVYRSRAVLIAAGLGAFEPrKLPQLGNID 144
Cdd:COG1249 82 lmarkdkvvdrLRGGVEELLKKNGVDVIRGRA----RFVDPHTVEV--TGGETLTADHIVIATGSRPRVP-PIPGLDEVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 145 HLTGSSVYyAVKSVdnfkGKRVVIVGGGdsaldwTVGL-----LKNAES-VTLVHRAKEFQGH-----GKTAHEveQAKA 213
Cdd:COG1249 155 VLTSDEAL-ELEEL----PKSLVVIGGG------YIGLefaqiFARLGSeVTLVERGDRLLPGedpeiSEALEK--ALEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 214 DGlIDVHLQTEVASIEESNGALThVHLRSSNGEEwTVEADRLLILIGFKSNLGPL----AGwdLELAEN-ALVVDSHMKT 288
Cdd:COG1249 222 EG-IDILTGAKVTSVEKTGDGVT-VTLEDGGGEE-AVEADKVLVATGRRPNTDGLgleaAG--VELDERgGIKVDEYLRT 296
|
330 340 350
....*....|....*....|....*....|....
gi 501494460 289 SVDGLYAAGDIAhypGKLKIIQTGLSEATMAVRH 322
Cdd:COG1249 297 SVPGIYAIGDVT---GGPQLAHVASAEGRVAAEN 327
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
82-322 |
1.64e-17 |
|
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: 82.17 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 82 AQAERYNPDVVLGEAVTKytkLDDGTFETRTNAGNVYRSRAVLIAAGLgafEPRKLP----QLGNIDHLTGSSVYYAVKS 157
Cdd:COG0446 44 ESFERKGIDVRTGTEVTA---IDPEAKTVTLRDGETLSYDKLVLATGA---RPRPPPipglDLPGVFTLRTLDDADALRE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 158 -VDNFKGKRVVIVGGG------DSALdwtvglLKNAESVTLVHRA----------------KEFQGHGktaheveqakad 214
Cdd:COG0446 118 aLKEFKGKRAVVIGGGpiglelAEAL------RKRGLKVTLVERAprllgvldpemaalleEELREHG------------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 215 glIDVHLQTEVASIEESNgaltHVHLRSSNGEEwtVEADRLLILIGFKSNLGPLAGWDLELAEN-ALVVDSHMKTSVDGL 293
Cdd:COG0446 180 --VELRLGETVVAIDGDD----KVAVTLTDGEE--IPADLVVVAPGVRPNTELAKDAGLALGERgWIKVDETLQTSDPDV 251
|
250 260
....*....|....*....|....*....
gi 501494460 294 YAAGDIAHYPGKLKIIQTGLSEATMAVRH 322
Cdd:COG0446 252 YAAGDCAEVPHPVTGKTVYIPLASAANKQ 280
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
15-306 |
2.54e-16 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 79.42 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 15 RDLTIIGGGPTGIFAAfqcgmnniscriiESMSQLGGQ-----LAAlypEKHI--------YDVAGfpEVPAIDLVESLW 81
Cdd:COG1251 2 MRIVIIGAGMAGVRAA-------------EELRKLDPDgeitvIGA---EPHPpynrpplsKVLAG--ETDEEDLLLRPA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 82 AQAERYNPDVVLGEAVTKytkLDDGTFETRTNAGNVYRSRAVLIAAGLgafEPRKLPQLGNidHLTGSSVYYAVKSVDNF 161
Cdd:COG1251 64 DFYEENGIDLRLGTRVTA---IDRAARTVTLADGETLPYDKLVLATGS---RPRVPPIPGA--DLPGVFTLRTLDDADAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 162 K-----GKRVVIVGGGdsaLdwtVGL-----LKNAE-SVTLVHRA-----------------KEFQGHGktaheveqaka 213
Cdd:COG1251 136 RaalapGKRVVVIGGG---L---IGLeaaaaLRKRGlEVTVVERAprllprqldeeagallqRLLEALG----------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 214 dglIDVHLQTEVASIEeSNGALTHVHLrsSNGEewTVEADRLLILIGFKSNLGPLAGWDLELaENALVVDSHMKTSVDGL 293
Cdd:COG1251 199 ---VEVRLGTGVTEIE-GDDRVTGVRL--ADGE--ELPADLVVVAIGVRPNTELARAAGLAV-DRGIVVDDYLRTSDPDI 269
|
330
....*....|...
gi 501494460 294 YAAGDIAHYPGKL 306
Cdd:COG1251 270 YAAGDCAEHPGPV 282
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
19-299 |
2.01e-15 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 77.47 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLAALYPE----KHIYDVAgfpevpaidlVESLWAQAERYNPDVVLG 94
Cdd:PRK12778 436 VIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYGIPEfrlpKKIVDVE----------IENLKKLGVKFETDVIVG 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 95 EAVTkYTKLDDGTFEtrtnagnvyrsrAVLIAAGLGafeprkLPQLGNI--DHLTG--SSVYYAVKS--VDNFK------ 162
Cdd:PRK12778 506 KTIT-IEELEEEGFK------------GIFIASGAG------LPNFMNIpgENSNGvmSSNEYLTRVnlMDAASpdsdtp 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 163 ---GKRVVIVGGGDSALDWTVGLLK-NAESVTLVHRAKEFQGHGKtAHEVEQAKADGLIDVHLQTEVASIEESNGALTHV 238
Cdd:PRK12778 567 ikfGKKVAVVGGGNTAMDSARTAKRlGAERVTIVYRRSEEEMPAR-LEEVKHAKEEGIEFLTLHNPIEYLADEKGWVKQV 645
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501494460 239 HL------------RSS----NGEEWTVEADRLLILIGFKSN-LGPLAGWDLELAE-NALVVDSHMKTSVDGLYAAGDI 299
Cdd:PRK12778 646 VLqkmelgepdasgRRRpvaiPGSTFTVDVDLVIVSVGVSPNpLVPSSIPGLELNRkGTIVVDEEMQSSIPGIYAGGDI 724
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
122-298 |
6.93e-14 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 72.50 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 122 AVLIaaGLGAFEPRKLPQLGniDHLTGssVYYAV-------KSVDNF--------KGKRVVIVGGGDSALDwTVG--LLK 184
Cdd:PRK12810 231 AVFL--GTGAYKPRDLGIPG--RDLDG--VHFAMdfliqntRRVLGDetepfisaKGKHVVVIGGGDTGMD-CVGtaIRQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 185 NAESVTLV--------HRAKEFQ-GHGKTAHEVEQAKADG-LIDVHLQTEvaSIEESNGALTHVH-----LRSSN----- 244
Cdd:PRK12810 304 GAKSVTQRdimpmppsRRNKNNPwPYWPMKLEVSNAHEEGvEREFNVQTK--EFEGENGKVTGVKvvrteLGEGDfepve 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 245 GEEWTVEADRLLILIGFksnLGPLAGW----DLELAE--NALVVDSHMKTSVDGLYAAGD 298
Cdd:PRK12810 382 GSEFVLPADLVLLAMGF---TGPEAGLlaqfGVELDErgRVAAPDNAYQTSNPKVFAAGD 438
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
16-312 |
2.75e-13 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 70.57 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 16 DLTIIGGGPTGIFAAFQCGMNNISCRIIesMSQLGGQLAalypekhiyDVAG---FPEVPAID---LVESLWAQAERYNP 89
Cdd:PRK15317 213 DVLVVGGGPAGAAAAIYAARKGIRTGIV--AERFGGQVL---------DTMGienFISVPETEgpkLAAALEEHVKEYDV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 90 DVVLGEAVTKYTKlDDGTFETRTNAGNVYRSRAVLIAagLGAfEPRKLpqlgNI---DHLTGSSVYYAvKSVDN--FKGK 164
Cdd:PRK15317 282 DIMNLQRASKLEP-AAGLIEVELANGAVLKAKTVILA--TGA-RWRNM----NVpgeDEYRNKGVAYC-PHCDGplFKGK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 165 RVVIVGGGDS----ALDwtvgLLKNAESVTLVHRAKEFQghgktAHEVEQAKADGL--IDVHLQTEVASIEESNGALTHV 238
Cdd:PRK15317 353 RVAVIGGGNSgveaAID----LAGIVKHVTVLEFAPELK-----ADQVLQDKLRSLpnVTIITNAQTTEVTGDGDKVTGL 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501494460 239 HLRS-SNGEEWTVEADRLLILIGfksnLGPLAGW---DLELAE-NALVVDSHMKTSVDGLYAAGDIAHYPGKLKIIQTG 312
Cdd:PRK15317 424 TYKDrTTGEEHHLELEGVFVQIG----LVPNTEWlkgTVELNRrGEIIVDARGATSVPGVFAAGDCTTVPYKQIIIAMG 498
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
122-316 |
9.97e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 68.48 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 122 AVLIAAGlgAFEPRKLpqlgNIDHLTGSSVYYAV----------------KSVDNFKGKRVVIVGGGDSALDWTV-GLLK 184
Cdd:PRK12770 121 AVLIATG--TWKSRKL----GIPGEDLPGVYSALeylfriraaklgylpwEKVPPVEGKKVVVVGAGLTAVDAALeAVLL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 185 NAESVTLVHR-AKEFQGHGKtaHEVEQAKADGLIDVHLQTEVASIEEsnGALTHVHLRSSN----------------GEE 247
Cdd:PRK12770 195 GAEKVYLAYRrTINEAPAGK--YEIERLIARGVEFLELVTPVRIIGE--GRVEGVELAKMRlgepdesgrprpvpipGSE 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501494460 248 WTVEADRLLILIGfKSNLGPLAGWDLELAEN---ALVVDSHMKTSVDGLYAAGDIAHYPGKL-KIIQTGLSEA 316
Cdd:PRK12770 271 FVLEADTVVFAIG-EIPTPPFAKECLGIELNrkgEIVVDEKHMTSREGVFAAGDVVTGPSKIgKAIKSGLRAA 342
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
19-194 |
1.16e-12 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 68.35 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQ-LAALYP------EKHIYdvaGFPEVPAIDLVESLWAQ-------- 83
Cdd:COG2072 11 VIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTwRDNRYPglrldtPSHLY---SLPFFPNWSDDPDFPTGdeilayle 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 84 --AERYN--PDVVLGEAVTKYT-KLDDGTFETRTNAGNVYRSRAVLIAAGlgAFEPRKLPQLGNIDHLTG----SSVYya 154
Cdd:COG2072 88 ayADKFGlrRPIRFGTEVTSARwDEADGRWTVTTDDGETLTARFVVVATG--PLSRPKIPDIPGLEDFAGeqlhSADW-- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501494460 155 vKSVDNFKGKRVVIVGGGDSALDWTVGLLKNAESVTLVHR 194
Cdd:COG2072 164 -RNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQR 202
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
19-322 |
1.92e-12 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 67.98 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLaaLYpekhiydvaGFPE--VP------AIDLVESLWAQAeRYNPD 90
Cdd:PRK12771 142 VIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMM--RY---------GIPAyrLPrevldaEIQRILDLGVEV-RLGVR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 91 VvlGEAVTKytKLDDGTFEtrtnagnvyrsrAVLIAagLGAFEPRKLPqlgnIDHLTGSSVYYAVKSVDNFK-------G 163
Cdd:PRK12771 210 V--GEDITL--EQLEGEFD------------AVFVA--IGAQLGKRLP----IPGEDAAGVLDAVDFLRAVGegeppflG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 164 KRVVIVGGGDSALD-WTVGLLKNAESVTLVHRAK--EFQGHgktAHEVEQAKADGlIDVHLQTEVASIEESNGALTHV-- 238
Cdd:PRK12771 268 KRVVVIGGGNTAMDaARTARRLGAEEVTIVYRRTreDMPAH---DEEIEEALREG-VEINWLRTPVEIEGDENGATGLrv 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 239 ----------HLRSS--NGEEWTVEADRLLILIGFKSNLGPLAGWD-LELAENALVVD-SHMKTSVDGLYAAGDiahypg 304
Cdd:PRK12771 344 itvekmeldeDGRPSpvTGEEETLEADLVVLAIGQDIDSAGLESVPgVEVGRGVVQVDpNFMMTGRPGVFAGGD------ 417
|
330
....*....|....*...
gi 501494460 305 klkiIQTGLSEATMAVRH 322
Cdd:PRK12771 418 ----MVPGPRTVTTAIGH 431
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
19-299 |
4.42e-12 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 66.97 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLaalypekhiydVAGFPE--VPAIDLV----ESLWAQAERYNPDVV 92
Cdd:PRK12831 145 VIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVL-----------VYGIPEfrLPKETVVkkeiENIKKLGVKIETNVV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 93 LGEAVTKYTKLDDGTFEtrtnagnvyrsrAVLIAAGLGafeprkLPQLGNIDHLTGSSVYYA------VKSVDNFK---- 162
Cdd:PRK12831 214 VGKTVTIDELLEEEGFD------------AVFIGSGAG------LPKFMGIPGENLNGVFSAnefltrVNLMKAYKpeyd 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 163 -----GKRVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEFQGHGKtAHEVEQAKADGLIDVHLQTEVASIEESNGALTH 237
Cdd:PRK12831 276 tpikvGKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRSEEELPAR-VEEVHHAKEEGVIFDLLTNPVEILGDENGWVKG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 238 VHL----------------RSSNGEEWTVEADRLLILIGFKSNlgPL---AGWDLELAENA-LVVDSHM-KTSVDGLYAA 296
Cdd:PRK12831 355 MKCikmelgepdasgrrrpVEIEGSEFVLEVDTVIMSLGTSPN--PLissTTKGLKINKRGcIVADEETgLTSKEGVFAG 432
|
...
gi 501494460 297 GDI 299
Cdd:PRK12831 433 GDA 435
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
139-300 |
2.77e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.21 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 139 QLGNIDHLT----GSSVYYAVKSVDNfkgKRVVIVGGGDSALDWTVGLLKNAESVTLVHRA---------KEFqghgkTA 205
Cdd:PRK09564 124 NLENVYTLKsmedGLALKELLKDEEI---KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrilpdsfdKEI-----TD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 206 HEVEQAKADGlIDVHLQTEVASIEeSNGALTHVhlRSSNGEewtVEADRLLILIGFKSNLGPLAGWDLELAEN-ALVVDS 284
Cdd:PRK09564 196 VMEEELRENG-VELHLNEFVKSLI-GEDKVEGV--VTDKGE---YEADVVIVATGVKPNTEFLEDTGLKTLKNgAIIVDE 268
|
170
....*....|....*.
gi 501494460 285 HMKTSVDGLYAAGDIA 300
Cdd:PRK09564 269 YGETSIENIYAAGDCA 284
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
8-312 |
5.60e-10 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 59.69 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 8 TTDHQDirdLTIIGGGPTGIFAAFQCGMNNISCRIIESMSQlGGQLAAlypEKHIYDVAGFP-EVPAIDLVESLWAQAER 86
Cdd:PRK10262 3 TTKHSK---LLILGSGPAGYTAAVYAARANLQPVLITGMEK-GGQLTT---TTEVENWPGDPnDLTGPLLMERMHEHATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 87 YNPDVVLGEavTKYTKLDDGTFETRTNAGNvYRSRAVLIAAGLGAfeprKLPQLGNIDHLTGSSVYyAVKSVDNF--KGK 164
Cdd:PRK10262 76 FETEIIFDH--INKVDLQNRPFRLTGDSGE-YTCDALIIATGASA----RYLGLPSEEAFKGRGVS-ACATCDGFfyRNQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 165 RVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEFQGHGKTAHEVEQAKADGLIDVHLQTEVASIEESNGALTHVHLRSSN 244
Cdd:PRK10262 148 KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQ 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501494460 245 GEE--WTVEADRLLILIGFKSNLGPLAGwDLELAENALVVDSHM-----KTSVDGLYAAGDIAHYPGKLKIIQTG 312
Cdd:PRK10262 228 NSDniESLDVAGLFVAIGHSPNTAIFEG-QLELENGYIKVQSGIhgnatQTSIPGVFAAGDVMDHIYRQAITSAG 301
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
19-298 |
7.51e-10 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 60.13 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLAalypekhiYDVAGF--PEvPAIDL-VESLWAQAERYNPDVVLGE 95
Cdd:PRK12814 198 IIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMR--------YGIPRFrlPE-SVIDAdIAPLRAMGAEFRFNTVFGR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 96 avtkytkldDGTFETRTNAGNvyrsrAVLIAagLGAFEPRKLPQLGniDHLTG--SSVYYAVKSVDNFK---GKRVVIVG 170
Cdd:PRK12814 269 ---------DITLEELQKEFD-----AVLLA--VGAQKASKMGIPG--EELPGviSGIDFLRNVALGTAlhpGKKVVVIG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 171 GGDSALDWTVGLLK-NAESVTLVHR--AKEFQGHgktAHEVEQAKADGlIDVHLQTEVASIEESNGALTHVHLRSSNGE- 246
Cdd:PRK12814 331 GGNTAIDAARTALRlGAESVTILYRrtREEMPAN---RAEIEEALAEG-VSLRELAAPVSIERSEGGLELTAIKMQQGEp 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501494460 247 --------------EWTVEADRLLILIGFKSNLGPLAGWDLELAENALVV--DSHMKTSVDGLYAAGD 298
Cdd:PRK12814 407 desgrrrpvpvegsEFTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKvdPETLQTSVAGVFAGGD 474
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
123-299 |
2.63e-09 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 58.29 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 123 VLIAAGLGAFEPRkLPQLGNIDHLTGSSVYyavkSVDnFKGKRVVIVGGGdsaldwTVGLlknaE----------SVTLV 192
Cdd:PRK06370 137 IFINTGARAAIPP-IPGLDEVGYLTNETIF----SLD-ELPEHLVIIGGG------YIGL----EfaqmfrrfgsEVTVI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 193 HRAKEFQGH--GKTAHEVEQA-KADGlIDVHLQTEVASIEESNGALThVHLRSSNGEEwTVEADRLLILIGFKSNLGPLa 269
Cdd:PRK06370 201 ERGPRLLPRedEDVAAAVREIlEREG-IDVRLNAECIRVERDGDGIA-VGLDCNGGAP-EITGSHILVAVGRVPNTDDL- 276
|
170 180 190
....*....|....*....|....*....|....*.
gi 501494460 270 gwDLELA------ENALVVDSHMKTSVDGLYAAGDI 299
Cdd:PRK06370 277 --GLEAAgvetdaRGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
162-305 |
1.33e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 55.91 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 162 KGKRVVIVGGGDSAL-------DWTVGLLKNAE------SVTLVHRAKE-FQGHGKTAHE--VEQAKADGlIDVHLQTEV 225
Cdd:COG1252 148 RLLTIVVVGGGPTGVelagelaELLRKLLRYPGidpdkvRITLVEAGPRiLPGLGEKLSEaaEKELEKRG-VEVHTGTRV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 226 ASIEEsngalTHVHLrsSNGEEwtVEADRLLILIGFKSNlGPLAGWDLELAE-NALVVDSHMKT-SVDGLYAAGDIAHYP 303
Cdd:COG1252 227 TEVDA-----DGVTL--EDGEE--IPADTVIWAAGVKAP-PLLADLGLPTDRrGRVLVDPTLQVpGHPNVFAIGDCAAVP 296
|
..
gi 501494460 304 GK 305
Cdd:COG1252 297 DP 298
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
16-299 |
2.99e-08 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 55.16 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 16 DLTIIGGGPTGIFAAFQCGMNNISCRIIESmSQLGGQL-------------AALYPEkHIYDVA---GF-PEVPAID--- 75
Cdd:PRK06116 6 DLIVIGGGSGGIASANRAAMYGAKVALIEA-KRLGGTCvnvgcvpkklmwyGAQIAE-AFHDYApgyGFdVTENKFDwak 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 76 LVESLWAQAER-----------YNPDVVLGEAvtkyTKLDDGTFETrtnAGNVYRSRAVLIAAGlGafEPRKlPQLGNID 144
Cdd:PRK06116 84 LIANRDAYIDRlhgsyrnglenNGVDLIEGFA----RFVDAHTVEV---NGERYTADHILIATG-G--RPSI-PDIPGAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 145 HLTGSSVYYAVKSVDnfkgKRVVIVGGGDSALDWTvGLLKNAES-VTLVHRAKEF---QGHGKTAHEVEQAKADGlIDVH 220
Cdd:PRK06116 153 YGITSDGFFALEELP----KRVAVVGAGYIAVEFA-GVLNGLGSeTHLFVRGDAPlrgFDPDIRETLVEEMEKKG-IRLH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 221 LQTEVASIE-ESNGALThVHLrsSNGEewTVEADRLLILIGFK---SNLGpLAGWDLELAEN-ALVVDSHMKTSVDGLYA 295
Cdd:PRK06116 227 TNAVPKAVEkNADGSLT-LTL--EDGE--TLTVDCLIWAIGREpntDGLG-LENAGVKLNEKgYIIVDEYQNTNVPGIYA 300
|
....
gi 501494460 296 AGDI 299
Cdd:PRK06116 301 VGDV 304
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
162-301 |
4.62e-08 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 54.65 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 162 KGKRVVIVGGGDSALD-WTVGLLKNAESVTLVHRAKEFQGHGkTAHEVEQAKADGlIDVHLQTEVASI-EESNGALTHVH 239
Cdd:PRK12809 450 EGKRVVVLGGGDTTMDcLRTSIRLNAASVTCAYRRDEVSMPG-SRKEVVNAREEG-VEFQFNVQPQYIaCDEDGRLTAVG 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 240 L-RSSNGE---------------EWTVEADRLLILIGFKSNLGP-LAGWDLELAENALVVDSHM-----KTSVDGLYAAG 297
Cdd:PRK12809 528 LiRTAMGEpgpdgrrrprpvagsEFELPADVLIMAFGFQAHAMPwLQGSGIKLDKWGLIQTGDVgylptQTHLKKVFAGG 607
|
....
gi 501494460 298 DIAH 301
Cdd:PRK12809 608 DAVH 611
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
16-320 |
7.97e-08 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 53.61 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 16 DLTIIGGGPTGIFAAF---QCGMnniSCRIIESmSQLGGQ------------LAAlypeKHIYD----------VAGFPE 70
Cdd:PRK06416 6 DVIVIGAGPGGYVAAIraaQLGL---KVAIVEK-EKLGGTclnrgcipskalLHA----AERADearhsedfgiKAENVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 71 V--PAI-----DLVESLWA----QAERYNPDVVLGEAvtkytKLDD-GTFETRTNAGN-VYRSRAVLIAAGLgafEPRKL 137
Cdd:PRK06416 78 IdfKKVqewknGVVNRLTGgvegLLKKNKVDIIRGEA-----KLVDpNTVRVMTEDGEqTYTAKNIILATGS---RPREL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 138 PQLgNIDHltgssvyyavKSVDNFKG--------KRVVIVGGG------DSAldWT--------VGLLKN------AESV 189
Cdd:PRK06416 150 PGI-EIDG----------RVIWTSDEalnldevpKSLVVIGGGyigvefASA--YAslgaevtiVEALPRilpgedKEIS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 190 TLVHRAKEFQGhgktaheveqakadglIDVHLQTEVASIEESNGALThVHLrSSNGEEWTVEADRLLILIGFK---SNLG 266
Cdd:PRK06416 217 KLAERALKKRG----------------IKIKTGAKAKKVEQTDDGVT-VTL-EDGGKEETLEADYVLVAVGRRpntENLG 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 501494460 267 pLAGWDLELAENALVVDSHMKTSVDGLYAAGDIAhypGKLKIIQTGLSEATMAV 320
Cdd:PRK06416 279 -LEELGVKTDRGFIEVDEQLRTNVPNIYAIGDIV---GGPMLAHKASAEGIIAA 328
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
16-299 |
8.34e-08 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 53.64 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 16 DLTIIGGGPTGIFAAFQCGMNNISCRIIESmSQLGGQLAA---------LYPEKHIYDVAGFPE------VPAIDLVESL 80
Cdd:PRK06292 5 DVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNvgcipskalIAAAEAFHEAKHAEEfgihadGPKIDFKKVM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 81 -WAQAER--YNPDVVLGE----AVTKYTK----LDDGTFETrtnAGNVYRSRAVLIAAGlgafepRKLPQLGNIDHLTGS 149
Cdd:PRK06292 84 aRVRRERdrFVGGVVEGLekkpKIDKIKGtarfVDPNTVEV---NGERIEAKNIVIATG------SRVPPIPGVWLILGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 150 SVYyavKSVDNFK----GKRVVIVGGGdsaldwTVGL-LKNAES-----VTLVHRAKEFQGH-----GKTAHEVEQAKad 214
Cdd:PRK06292 155 RLL---TSDDAFEldklPKSLAVIGGG------VIGLeLGQALSrlgvkVTVFERGDRILPLedpevSKQAQKILSKE-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 215 glIDVHLQTEVASIEESNGALthVHLRSSNGEEWTVEADRLLILIGFKSN---LGpLAGWDLELAENALV-VDSHMKTSV 290
Cdd:PRK06292 224 --FKIKLGAKVTSVEKSGDEK--VEELEKGGKTETIEADYVLVATGRRPNtdgLG-LENTGIELDERGRPvVDEHTQTSV 298
|
....*....
gi 501494460 291 DGLYAAGDI 299
Cdd:PRK06292 299 PGIYAAGDV 307
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
164-324 |
8.48e-08 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 53.42 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 164 KRVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEFQGHGKTA-HE--VEQAKADglIDVHLQTEVASIEESNGALThvhL 240
Cdd:PRK07846 167 ESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDiSErfTELASKR--WDVRLGRNVVGVSQDGSGVT---L 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 241 RSSNGEewTVEADRLLILIGFKSN---LGPLAGwDLELAENALV-VDSHMKTSVDGLYAAGDIAHyPGKLKIIQTglSEA 316
Cdd:PRK07846 242 RLDDGS--TVEADVLLVATGRVPNgdlLDAAAA-GVDVDEDGRVvVDEYQRTSAEGVFALGDVSS-PYQLKHVAN--HEA 315
|
....*...
gi 501494460 317 TmAVRHSL 324
Cdd:PRK07846 316 R-VVQHNL 322
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
19-320 |
1.14e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 53.33 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLAALYpekhiydvAGFPEV-PAIDLVESLWAQAERyNP--DVVLG- 94
Cdd:COG1148 145 VIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLH--------KTFPGLdCPQCILEPLIAEVEA-NPniTVYTGa 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 95 --EAVTKY-----TKLDDGTFETRT-NAGnvyrsrAVLIAAGLGAFEPRKLPQLG-----------------NIDHLTGS 149
Cdd:COG1148 216 evEEVSGYvgnftVTIKKGPREEIEiEVG------AIVLATGFKPYDPTKLGEYGygkypnvitnlelerllAAGKILRP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 150 SvyyavksvDNFKGKRVVI---VGGGDSaldwTVGL-----------LKNAesvtlvHRAKEFQGH-------------G 202
Cdd:COG1148 290 S--------DGKEPKSVAFiqcVGSRDE----ENGLpycsrvccmyaLKQA------LYLKEKNPDadvyifyrdirtyG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 203 KTAHEVEQAKADGLIdvHLQTEVASIEES-NGALTHVHLRSSNGEEWTVEADrLLIL-IGFKSNLG--PLAGW-DLELAE 277
Cdd:COG1148 352 KYEEFYRRAREDGVR--FIRGRVAEIEEDeGGKLVVTVEDTLLGEPVEIEAD-LVVLaTGMVPSEDneELAKLlKLPLDQ 428
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 501494460 278 NALVVDSHMK-----TSVDGLYAAGdIAHYPgklKIIQTGLSEATMAV 320
Cdd:COG1148 429 DGFFLEAHPKlrpveTATDGIFLAG-AAHGP---KDIPESIAQATAAA 472
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
164-303 |
3.07e-07 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 52.08 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 164 KRVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEFQ------GHGKTAheveQAKADGlIDVHLQTEVASIEESNGALTh 237
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFredpaiGEAVTA----AFRAEG-IEVLEHTQASQVAHVDGEFV- 344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 238 vhLRSSNGEewtVEADRLLILIGFKSNLGPL----AGWDLElAENALVVDSHMKTSVDGLYAAGDIAHYP 303
Cdd:PRK13748 345 --LTTGHGE---LRADKLLVATGRAPNTRSLaldaAGVTVN-AQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
217-303 |
3.34e-07 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 51.85 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 217 IDVHLQTEVASIEESNGALThVHLRSSNGEEWTVEADRLLILIGFKSNLGPL----AGwdLELAEN-ALVVDSHMKTSVD 291
Cdd:PRK06327 239 LDIHLGVKIGEIKTGGKGVS-VAYTDADGEAQTLEVDKLIVSIGRVPNTDGLgleaVG--LKLDERgFIPVDDHCRTNVP 315
|
90
....*....|..
gi 501494460 292 GLYAAGDIAHYP 303
Cdd:PRK06327 316 NVYAIGDVVRGP 327
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
17-332 |
6.18e-07 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 51.48 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 17 LTIIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLAalypekhiYDVAGFpEVP--AIDL-VESLWAQAERYNPDVVL 93
Cdd:PRK12775 433 VAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQ--------YGIPSF-RLPrdIIDReVQRLVDIGVKIETNKVI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 94 GEAVTKYTKLDDGTFEtrtnagnvyrsrAVLIAAGLGAfeprklPQLGNIDHLTGSSVYYAVKSV--------DNFK--- 162
Cdd:PRK12775 504 GKTFTVPQLMNDKGFD------------AVFLGVGAGA------PTFLGIPGEFAGQVYSANEFLtrvnlmggDKFPfld 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 163 -----GKRVVIVGGGDSALD-WTVGLLKNAESVTLVHRAKEFQGHGKTaHEVEQAKADGLIDVHLQTEVASIEESNGALT 236
Cdd:PRK12775 566 tpislGKSVVVIGAGNTAMDcLRVAKRLGAPTVRCVYRRSEAEAPARI-EEIRHAKEEGIDFFFLHSPVEIYVDAEGSVR 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 237 HVHLRS---------------SNGEEWTVEADRLLILIGFKSNlgPLAG----------WDlELAENALVVDSHMKTSVD 291
Cdd:PRK12775 645 GMKVEEmelgepdekgrrkpmPTGEFKDLECDTVIYALGTKAN--PIITqstpglalnkWG-NIAADDGKLESTQSTNLP 721
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 501494460 292 GLYAAGDIAhyPGKLKIIqTGLSEATMAVRHSLSYIKPGEK 332
Cdd:PRK12775 722 GVFAGGDIV--TGGATVI-LAMGAGRRAARSIATYLRLGKK 759
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
115-299 |
1.60e-06 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 49.87 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 115 GNVYRSRAVLIAAGLGAFeprkLPQLGNIDHLTGSSVYYAVKSvdnfKGKRVVIVGGGDSALDWTvGLLK--NAESVTLV 192
Cdd:PLN02546 212 GKLYTARNILIAVGGRPF----IPDIPGIEHAIDSDAALDLPS----KPEKIAIVGGGYIALEFA-GIFNglKSDVHVFI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 193 HRAKEFQGHGKTAHE--VEQAKADGlIDVHL-QTEVASIEESNGALThvhLRSSNGeewTVEA-DRLLILIGFK---SNL 265
Cdd:PLN02546 283 RQKKVLRGFDEEVRDfvAEQMSLRG-IEFHTeESPQAIIKSADGSLS---LKTNKG---TVEGfSHVMFATGRKpntKNL 355
|
170 180 190
....*....|....*....|....*....|....*
gi 501494460 266 GpLAGWDLELAEN-ALVVDSHMKTSVDGLYAAGDI 299
Cdd:PLN02546 356 G-LEEVGVKMDKNgAIEVDEYSRTSVPSIWAVGDV 389
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
164-306 |
4.18e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 47.99 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 164 KRVVIVGGG----DSALDwtvgLLKNAESVTLVHRAK--------EFqghgkTAHEVEQAKADGLIDVHLQTEVASIEES 231
Cdd:PRK04965 142 QRVLVVGGGligtELAMD----LCRAGKAVTLVDNAAsllaslmpPE-----VSSRLQHRLTEMGVHLLLKSQLQGLEKT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 232 NGALThvhLRSSNGEewTVEADRLLILIGFKSNLGplagwdleLAENA-------LVVDSHMKTSVDGLYAAGDIAHYPG 304
Cdd:PRK04965 213 DSGIR---ATLDSGR--SIEVDAVIAAAGLRPNTA--------LARRAglavnrgIVVDSYLQTSAPDIYALGDCAEING 279
|
..
gi 501494460 305 KL 306
Cdd:PRK04965 280 QV 281
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
165-236 |
5.69e-06 |
|
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: 43.73 E-value: 5.69e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501494460 165 RVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEF-QGHGKTAHEV--EQAKADGlIDVHLQTEVASIEESNGALT 236
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLlPGFDPEIAKIlqEKLEKNG-IEFLLNTTVEAIEGNGDGVV 74
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
115-300 |
9.86e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 47.23 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 115 GNVYRSRAVLIAAGLGAfepRKLPQLgniDHLtGSSVYyAVKSVDNF--------KGKRVVIVGGGDSALDWTVGLLKNA 186
Cdd:PRK09754 96 GESWHWDQLFIATGAAA---RPLPLL---DAL-GERCF-TLRHAGDAarlrevlqPERSVVIVGAGTIGLELAASATQRR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 187 ESVTLVHRAKEFQGhgKTAHEVEQakaDGLIDVH--------LQTEVASIEESNgaltHVHLRSSNGEewTVEADRLLIL 258
Cdd:PRK09754 168 CKVTVIELAATVMG--RNAPPPVQ---RYLLQRHqqagvrilLNNAIEHVVDGE----KVELTLQSGE--TLQADVVIYG 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501494460 259 IG--FKSNLGPLAGWDlelAENALVVDSHMKTSVDGLYAAGDIA 300
Cdd:PRK09754 237 IGisANDQLAREANLD---TANGIVIDEACRTCDPAIFAGGDVA 277
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
158-302 |
4.45e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 45.16 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 158 VDNFKGKRVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEFqgHGKTAHEVEQAKADGL----IDVHLQTEVASIEESNg 233
Cdd:PRK13512 143 IKANQVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKI--NKLMDADMNQPILDELdkreIPYRLNEEIDAINGNE- 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501494460 234 althVHLRSSNGEEWtveaDRLLILIGFKSNLGPLAGWDLELAENALV-VDSHMKTSVDGLYAAGDIA--HY 302
Cdd:PRK13512 220 ----VTFKSGKVEHY----DMIIEGVGTHPNSKFIESSNIKLDDKGFIpVNDKFETNVPNIYAIGDIItsHY 283
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
15-141 |
6.17e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 44.49 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 15 RDLTIIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQL----------------------------AALYPEKHIYD-- 64
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKIlisgggrcnvtnlseepdnflsrypgnpKFLKSALSRFTpw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 65 -----VAG-------------FP-EVPAIDLVESLWAQAERYNPDVVLGEAVTKYTKLDDGTFETRTNaGNVYRSRAVLI 125
Cdd:pfam03486 81 dfiafFESlgvplkeedhgrlFPdSDKASDIVDALLNELKELGVKIRLRTRVLSVEKDDDGRFRVKTG-GEELEADSLVL 159
|
170
....*....|....*.
gi 501494460 126 AAGLGAFeprklPQLG 141
Cdd:pfam03486 160 ATGGLSW-----PKTG 170
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
164-299 |
1.54e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 43.20 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 164 KRVVIVGGGDSALDWTVGLLKNAESVTLVHRAKEFQGhgKTAHEVEQAKADGL----IDVHLQTEVASIEESNGALthvh 239
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP--REEPSVAALAKQYMeedgITFLLNAHTTEVKNDGDQV---- 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501494460 240 LRSSNGEEWTVEAdrLLILIGFKSNLGPLA--GWDLELAEN-ALVVDSHMKTSVDGLYAAGDI 299
Cdd:PRK07251 232 LVVTEDETYRFDA--LLYATGRKPNTEPLGleNTDIELTERgAIKVDDYCQTSVPGVFAVGDV 292
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
19-294 |
2.82e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 42.81 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQLAalypekhiydvagFpEVPAIDLVESLWAQAE----------RYN 88
Cdd:PRK12769 332 IIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLLT-------------F-GIPAFKLDKSLLARRReifsamgiefELN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 89 PDVvlGEAVTKYTKLDDgtFETRTNAGNVYRSravlIAAGL------GAFEprKLPQL-GNIDHLTGSSVYYAVKSVDNf 161
Cdd:PRK12769 398 CEV--GKDISLESLLED--YDAVFVGVGTYRS----MKAGLpnedapGVYD--ALPFLiANTKQVMGLEELPEEPFINT- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 162 KGKRVVIVGGGDSALDWT-VGLLKNAESVTLVHRAKEFQGHGkTAHEVEQAKADGlidVHLQTEVASIE---ESNGALTH 237
Cdd:PRK12769 467 AGLNVVVLGGGDTAMDCVrTALRHGASNVTCAYRRDEANMPG-SKKEVKNAREEG---ANFEFNVQPVAlelNEQGHVCG 542
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501494460 238 VH-LRSSNGE---------------EWTVEADRLLILIGFKSNLGPlagWdleLAENALVVDS--HMKTSVDGLY 294
Cdd:PRK12769 543 IRfLRTRLGEpdaqgrrrpvpipgsEFVMPADAVIMAFGFNPHGMP---W---LESHGVTVDKwgRIIADVESQY 611
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
19-141 |
5.19e-04 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 41.81 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 19 IIGGGPTGIFAAFQCGMNNISCRIIESMSQLGGQL------------AALYPEKhiydVAGFPEVP-------------- 72
Cdd:TIGR00275 2 IIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKLlisgggrcnltnSCPTPEF----VAYYPRNGkflrsalsrfsnkd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 73 AIDLVESL-------------------------WAQ-AERYNPDVVLGEAVTKYTKlDDGTFETRTNAGnVYRSRAVLIA 126
Cdd:TIGR00275 78 LIDFFESLglelkveedgrvfpcsdsaadvldaLLNeLKELGVEILTNSKVKSIEK-EDGGFGVETSGG-EYEADKVIIA 155
|
170
....*....|....*
gi 501494460 127 AGLGAFeprklPQLG 141
Cdd:TIGR00275 156 TGGLSY-----PQLG 165
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
164-299 |
5.61e-04 |
|
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: 41.50 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 164 KRVVIVGGGDSALDWTvGLLkNAE-----SVTLVHRAKE-FQGHGKTAHE--VEQAKADGlIDVHLQTEVASIEESNGAL 235
Cdd:TIGR01423 188 RRVLTVGGGFISVEFA-GIF-NAYkprggKVTLCYRNNMiLRGFDSTLRKelTKQLRANG-INIMTNENPAKVTLNADGS 264
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501494460 236 THVHLRSSNgeewTVEADRLLILIGF--KSNLGPLAGWDLELAEN-ALVVDSHMKTSVDGLYAAGDI 299
Cdd:TIGR01423 265 KHVTFESGK----TLDVDVVMMAIGRvpRTQTLQLDKVGVELTKKgAIQVDEFSRTNVPNIYAIGDV 327
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
14-185 |
6.33e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 41.48 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 14 IRDLTIIGGGPTGIFAAFQC---GMNNISCRIIESMSQLGGQLAalY---PEKHIYDVAG-----FPEVPAiDLVESLWA 82
Cdd:COG4529 5 RKRIAIIGGGASGTALAIHLlrrAPEPLRITLFEPRPELGRGVA--YstdSPEHLLNVPAgrmsaFPDDPD-HFLRWLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 83 QAERYNPDV---------VLGE--------AVTKYTKL---------------DDGTFETRTNAGNVYRSRAVLIAagLG 130
Cdd:COG4529 82 NGARAAPAIdpdafvprrLFGEylrerlaeALARAPAGvrlrhiraevvdlerDDGGYRVTLADGETLRADAVVLA--TG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501494460 131 AFEPRKLPQLGNIDHLTGSSVY--YAVKSVDnfKGKRVVIVGGGDSALDWTVGLLKN 185
Cdd:COG4529 160 HPPPAPPPGLAAGSPRYIADPWppGALARIP--PDARVLIIGTGLTAIDVVLSLAAR 214
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
103-317 |
1.29e-03 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 40.57 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 103 LDDGTFETRTNAGNV--YRSRAVLIAAGLGAFEPrKLPqlGNIDHLTGSSVYyavkSVDNFKgKRVVIVGGGDSALDWTV 180
Cdd:PLN02507 149 VGPNEVEVTQLDGTKlrYTAKHILIATGSRAQRP-NIP--GKELAITSDEAL----SLEELP-KRAVVLGGGYIAVEFAS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 181 GLLKNAESVTLVHRAK-EFQGHGKTAHEVEQAKADGL-IDVHLQTEVASIEESNGALThvhLRSSNGEEwtVEADRLLIL 258
Cdd:PLN02507 221 IWRGMGATVDLFFRKElPLRGFDDEMRAVVARNLEGRgINLHPRTNLTQLTKTEGGIK---VITDHGEE--FVADVVLFA 295
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501494460 259 IGFKSNLGPL----AGWDLELAeNALVVDSHMKTSVDGLYAAGDIAHypgKLKIIQTGLSEAT 317
Cdd:PLN02507 296 TGRAPNTKRLnleaVGVELDKA-GAVKVDEYSRTNIPSIWAIGDVTN---RINLTPVALMEGT 354
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
81-198 |
6.84e-03 |
|
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold oxidoreductases that catalyze NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyzes the hydroxylation of L-ornithine at the N5 position, and L-lysine 6-monooxygenase, which catalyzes the hydroxylation of lysine at the N6 position (EC:1.14.13.59).
Pssm-ID: 433204 [Multi-domain] Cd Length: 338 Bit Score: 37.95 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 81 WAqAERYNPDVVLGEAVTK--YTKLDDGTF---ETRTNAGNV--YRSRAVLIAAGLGAFEPRKLPQLGNIDHltgSSVYY 153
Cdd:pfam13434 103 WA-ASHLPNRLRFGQEVESvePDAERGEPLlrvRVRDADGEEttFLARNLVLGTGGEPYIPECARGGERVFH---SSEYL 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 501494460 154 AVKSVDNfKGKRVVIVGGGDSALDWTVGLLK--NAESVTLVHRAKEF 198
Cdd:pfam13434 179 ERIDRLA-AKKRIAVVGSGQSAAEIFRDLLRrgPAYELTWVTRSPNF 224
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
217-303 |
8.66e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 37.83 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501494460 217 IDVHLQTEVASIE-ESNGALthVHLRSSNgeewTVEADRLLILIGFKSNLGplagwDLELaENA---------LVVDSHM 286
Cdd:PRK05249 231 VTIRHNEEVEKVEgGDDGVI--VHLKSGK----KIKADCLLYANGRTGNTD-----GLNL-ENAgleadsrgqLKVNENY 298
|
90
....*....|....*..
gi 501494460 287 KTSVDGLYAAGDIAHYP 303
Cdd:PRK05249 299 QTAVPHIYAVGDVIGFP 315
|
|
| |
