|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
40-320 |
2.86e-142 |
|
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: 411.94 E-value: 2.86e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQ 119
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 120 PVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRGVDKGGKATLLSAEHIVIATGGRPRYPtQVK 199
Cdd:TIGR01438 83 TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 200 GALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSIPLRGFDQQMSSLVTEHMESHGTQFLKGC 279
Cdd:TIGR01438 162 GAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQF 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15489159 280 VPSHIKKLPTNQLqVTWEDHASGKEdtGTFDTVLWAIGKDA 320
Cdd:TIGR01438 242 VPIKVEQIEAKVL-VEFTDSTNGIE--EEYDTVLLAIGRDA 279
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
40-318 |
1.28e-119 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 354.51 E-value: 1.28e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIR-DAHHYGWEVA 118
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 119 QpvQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRGVDKGGKATLlSAEHIVIATGGRPRYPTQV 198
Cdd:PTZ00052 86 S--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQEETI-TAKYILIATGGRPSIPEDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 199 KGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSIPLRGFDQQMSSLVTEHMESHGTQFLKG 278
Cdd:PTZ00052 163 PGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLEG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15489159 279 CVPSHIKKLpTNQLQVTWEDHAsgkedTGTFDTVLWAIGK 318
Cdd:PTZ00052 243 VVPINIEKM-DDKIKVLFSDGT-----TELFDTVLYATGR 276
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
40-321 |
5.92e-81 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 253.93 E-value: 5.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEpsprgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRD-AHHYGWEVA 118
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 119 QPvQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRgVDKggkaTLLSAEHIVIATGGRPRYPTqV 198
Cdd:PRK06116 76 EN-KFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVE-VNG----ERYTADHILIATGGRPSIPD-I 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 199 KGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRS-IPLRGFDQQMSSLVTEHMESHGTQFLK 277
Cdd:PRK06116 149 PGA-EYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15489159 278 GCVPSHIKKLPTNQLQVTWEDhasGKEDtgTFDTVLWAIGKDAA 321
Cdd:PRK06116 228 NAVPKAVEKNADGSLTLTLED---GETL--TVDCLIWAIGREPN 266
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
38-317 |
2.29e-70 |
|
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: 226.51 E-value: 2.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQLGKKVAVADyvepsprgtKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEV 117
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 118 AQPvQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRgVDKGgkaTLLSAEHIVIATGGRPRYPTQ 197
Cdd:COG1249 73 GAP-SVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVE-VTGG---ETLTADHIVIATGSRPRVPPI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 198 VKGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSIPLRGFDQQMSSLVTEHMESHGTQFL 276
Cdd:COG1249 148 PGLDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDIL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15489159 277 KGCVPSHIKKLPtNQLQVTWEDhaSGKEDTGTFDTVLWAIG 317
Cdd:COG1249 228 TGAKVTSVEKTG-DGVTVTLED--GGGEEAVEADKVLVATG 265
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
38-318 |
1.17e-66 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 217.02 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEpsprgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEV 117
Cdd:TIGR01421 1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKK---------LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 118 AQPVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRgVDKggkaTLLSAEHIVIATGGRPRYPTQ 197
Cdd:TIGR01421 72 NDENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVE-VNG----RDYTAPHILIATGGKPSFPEN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 198 VKGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMR-SIPLRGFDQQMSSLVTEHMESHGTQFL 276
Cdd:TIGR01421 147 IPGA-ELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVH 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15489159 277 KGCVPSHIKKLPTNQLQVTWEDHASgkedTGTFDTVLWAIGK 318
Cdd:TIGR01421 226 KLSKPVKVEKTVEGKLVIHFEDGKS----IDDVDELIWAIGR 263
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
40-318 |
5.26e-61 |
|
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]
Pssm-ID: 213618 [Multi-domain] Cd Length: 446 Bit Score: 201.96 E-value: 5.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVADyvepSPRgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQ 119
Cdd:TIGR01424 3 YDLFVIGAGSGGVRAARLAAALGAKVAIAE----EFR-----VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 120 pVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRGVDKGGKATllsAEHIVIATGGRPRYPtQVK 199
Cdd:TIGR01424 74 -ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKTYT---AEKILIAVGGRPPKP-ALP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 200 GAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMR-SIPLRGFDQQMSSLVTEHMESHGTQFLKG 278
Cdd:TIGR01424 149 GH-ELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILPE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15489159 279 CVPSHIKKLPTNQLQVTWEDHasgkedtGTF--DTVLWAIGK 318
Cdd:TIGR01424 228 DSITSISKDDDGRLKATLSKH-------EEIvaDVVLFATGR 262
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
29-318 |
8.08e-50 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 173.85 E-value: 8.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 29 GAASAAGGQQSFDLLVIGGGSGGLACAKEAAQLGKKVAVADY-VEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMI 107
Cdd:PLN02507 15 NADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 108 RDAHHYGWEVAQPVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRGVDKGGKATLLSAEHIVIA 187
Cdd:PLN02507 95 EDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 188 TGGRPRYPTqVKGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMR-SIPLRGFDQQMSSLVTE 266
Cdd:PLN02507 175 TGSRAQRPN-IPGK-ELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRAVVAR 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15489159 267 HMESHGTQFLKGCVPSHIKKLpTNQLQVTwEDHasGKEDTGtfDTVLWAIGK 318
Cdd:PLN02507 253 NLEGRGINLHPRTNLTQLTKT-EGGIKVI-TDH--GEEFVA--DVVLFATGR 298
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
40-317 |
3.11e-47 |
|
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: 162.10 E-value: 3.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVAdyvepsprgtkwGLGGTCVNVGCIPKKLMHQAAllgGMIRDAHHygwevaq 119
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA---EAPEIASL------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 120 pvqhnWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVrgvdkGGKATLLSAEHIVIATGGRPRYPTqVK 199
Cdd:pfam07992 59 -----WADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARPRLPP-IP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 200 GALEYG------ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSIPLRGFDQQMSSLVTEHMESHG 272
Cdd:pfam07992 128 GVELNVgflvrtLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNG 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15489159 273 TQFLKGCVPSHIKKLPTNQLQVTwedhasGKEDTGTFDTVLWAIG 317
Cdd:pfam07992 208 VEVRLGTSVKEIIGDGDGVEVIL------KDGTEIDADLVVVAIG 246
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
39-317 |
2.30e-46 |
|
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: 163.97 E-value: 2.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 39 SFDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEpsprgtKWGLGGTCVNVGCIPKK-LMHQAALLgGMIRDAHHYGWEV 117
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVAL---VE------KEYLGGTCLNVGCIPTKaLLHSAEVY-DEIKHAKDLGIEV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 118 AQpVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRgVDKGGKATLLSAEHIVIATGGRPRY-PT 196
Cdd:TIGR01350 71 EN-VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVS-VTGENGEETLEAKNIIIATGSRPRSlPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 197 QVKGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTV--MMRSIpLRGFDQQMSSLVTEHMESHGTQ 274
Cdd:TIGR01350 149 PFDFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVK 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15489159 275 FLKGCVPSHIKKlptNQLQVTWEDhASGKEDTGTFDTVLWAIG 317
Cdd:TIGR01350 228 ILTNTKVTAVEK---NDDQVTYEN-KGGETETLTGEKVLVAVG 266
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
38-317 |
3.75e-46 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 163.39 E-value: 3.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEpsprgtKWGLGGTCVNVGCIPKKlmhqaALL--GGMIRDAHH--- 112
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAI---VE------KEKLGGTCLNRGCIPSK-----ALLhaAERADEARHsed 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 113 YGWEvAQPVQHNWKtmaeAVQNH----VKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRgVDKGGKATLLSAEHIVIAT 188
Cdd:PRK06416 69 FGIK-AENVGIDFK----KVQEWkngvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVR-VMTEDGEQTYTAKNIILAT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 189 GGRPRYPtqvKGaLEYG----ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTV--MMRSIpLRGFDQQMSS 262
Cdd:PRK06416 143 GSRPREL---PG-IEIDgrviWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISK 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15489159 263 LVTEHMESHGTQFLKGcvpSHIKKLPTNQLQVTWEDHASGKEDTGTFDTVLWAIG 317
Cdd:PRK06416 218 LAERALKKRGIKIKTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVG 269
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
38-318 |
4.56e-45 |
|
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: 160.91 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQL-GKKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWE 116
Cdd:TIGR01423 2 KAFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 117 V-AQPVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRK-VKYFNIKASFVDEHTV---RGVD-KGGKATLLSAEHIVIATGG 190
Cdd:TIGR01423 82 FdRSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVlvrESADpKSAVKERLQAEHILLATGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 191 RPRYPtQVKGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTVMMRSIP-LRGFDQQMSSLVTE 266
Cdd:TIGR01423 162 WPQML-GIPG-IEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLRGFDSTLRKELTK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15489159 267 HMESHGTQFLKGCVPSHIKKLPTNQLQVTWEdhaSGKedTGTFDTVLWAIGK 318
Cdd:TIGR01423 240 QLRANGINIMTNENPAKVTLNADGSKHVTFE---SGK--TLDVDVVMMAIGR 286
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
38-317 |
1.35e-42 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 153.79 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPrgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEV 117
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVAL---IEKGP------LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 118 AQPVQhNWKTMAEAVQNHVKSLNWGH-RVQLQDRKVKYFNIKASFVDEHTVRgVDKggkaTLLSAEHIVIATGGR-PRYP 195
Cdd:PRK06292 73 DGPKI-DFKKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVE-VNG----ERIEAKNIVIATGSRvPPIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 196 TQVKGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTV--MMRSIpLRGFDQQMSSLVTEHMESHgT 273
Cdd:PRK06292 147 GVWLILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVfeRGDRI-LPLEDPEVSKQAQKILSKE-F 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15489159 274 QFLKGcvpSHIKKLPTNQLQVTWEDHASGKEDTGTFDTVLWAIG 317
Cdd:PRK06292 225 KIKLG---AKVTSVEKSGDEKVEELEKGGKTETIEADYVLVATG 265
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
8-318 |
5.31e-42 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 154.00 E-value: 5.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 8 ALRGPSRRFrprTRALTRGTRGAASAAGGQQS------FDLLVIGGGSGGLACAKEAAQLGKKVAVADyvepsprgtKWG 81
Cdd:PTZ00058 14 ALLNPSIKL---IRSFSFYHNLEASSAPTHLKkkprmvYDLIVIGGGSGGMAAARRAARNKAKVALVE---------KDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 82 LGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQPVqhNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASF 161
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 162 VDEHTV---------------------------RGVDKGGKatlLSAEHIVIATGGRPRYPtQVKGaLEYGITSDDIFWL 214
Cdd:PTZ00058 160 LSENQVlikkvsqvdgeadesdddevtivsagvSQLDDGQV---IEGKNILIAVGNKPIFP-DVKG-KEFTISSDDFFKI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 215 KEsPGKTLVVGASYVALECAGFLTGIGLDTTVMMR-SIPLRGFDQQMSSLVTEHMESHGTQFLKGCVPSHIKKLPTNQLQ 293
Cdd:PTZ00058 235 KE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLT 313
|
330 340
....*....|....*....|....*
gi 15489159 294 VTWEDhaSGKEDtgTFDTVLWAIGK 318
Cdd:PTZ00058 314 IYLSD--GRKYE--HFDYVIYCVGR 334
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
13-318 |
2.39e-41 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 151.95 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 13 SRRFRPRTRALTRGTR--GAASAAGGQQS-----FDLLVIGGGSGGLACAKEAAQLGKKVAVADY-VEPSPRGTKWGLGG 84
Cdd:PLN02546 46 TRLSSPRPLSHHHRRRsvSRAAAPNGAESerhydFDLFTIGAGSGGVRASRFASNFGASAAVCELpFATISSDTLGGVGG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 85 TCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQPVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDE 164
Cdd:PLN02546 126 TCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 165 HTvrgVDKGGKatLLSAEHIVIATGGRPRYPtQVKGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDT 244
Cdd:PLN02546 206 HT---VDVDGK--LYTARNILIAVGGRPFIP-DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDV 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15489159 245 TVMMRSIP-LRGFDQQMSSLVTEHMESHGTQFLKGCVPSHIKKLPTNQLQVTwedhaSGKEDTGTFDTVLWAIGK 318
Cdd:PLN02546 279 HVFIRQKKvLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLK-----TNKGTVEGFSHVMFATGR 348
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
37-317 |
3.02e-37 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 139.18 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 37 QQSFDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPrgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWE 116
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVAL---IERGL------LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 117 VAQPVQHNWKT----MAEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVDEHTVRgVDkggkATLLSAEHIVIATGG 190
Cdd:PRK06370 74 VGGPVSVDFKAvmarKRRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG----GETLRAKRIFINTGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 191 RPRYPtQVKGALEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSiP--LRGFDQQMSSLVTEH 267
Cdd:PRK06370 144 RAAIP-PIPGLDEVGyLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPREDEDVAAAVREI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15489159 268 MESHGTQFLKGCVPSHIKKLPTnqlQVTWEDHASGKEDTGTFDTVLWAIG 317
Cdd:PRK06370 222 LEREGIDVRLNAECIRVERDGD---GIAVGLDCNGGAPEITGSHILVAVG 268
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
37-317 |
4.84e-33 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 127.58 E-value: 4.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 37 QQSFDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPRgtkwgLGGTCVNVGCIPKKLMHQAAL-LGGMIRDAHHYGW 115
Cdd:PRK05249 3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAV---IERYRN-----VGGGCTHTGTIPSKALREAVLrLIGFNQNPLYSSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 116 EVAQPVqhnwkTM------AEAVQNHVKSLnwgHRVQLQDRKVKYFNIKASFVDEHTVRGVDKGGKATLLSAEHIVIATG 189
Cdd:PRK05249 75 RVKLRI-----TFadllarADHVINKQVEV---RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 190 GRPRYPTQVKGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSIPLRGFDQQMSSLVTEHM 268
Cdd:PRK05249 147 SRPYRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15489159 269 ESHGTQFLKGCVPSHIKKLptnqlqvtwEDH-----ASGKEDTGtfDTVLWAIG 317
Cdd:PRK05249 227 RDSGVTIRHNEEVEKVEGG---------DDGvivhlKSGKKIKA--DCLLYANG 269
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
40-278 |
3.53e-28 |
|
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: 114.44 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEpspRGTkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAhHYGWEVAQ 119
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAM---VE---RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKP-PFGGLAAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 120 P-------VQHNWKTMAEAVQNHVKSLnwghrvqLQDRKVKYFNIKASFVDEHTVRgVDkGGKATlLSAEHIVIATGGRP 192
Cdd:TIGR02053 71 VavdfgelLEGKREVVEELRHEKYEDV-------LSSYGVDYLRGRARFKDPKTVK-VD-LGREV-RGAKRFLIATGARP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 193 RYPtQVKGALEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRS-IPLRGFDQQMSSLVTEHMES 270
Cdd:TIGR02053 141 AIP-PIPGLKEAGyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAE 219
|
....*...
gi 15489159 271 HGTQFLKG 278
Cdd:TIGR02053 220 EGIEVVTS 227
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
40-271 |
6.41e-26 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 107.73 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAqlGKKVAVADyvepspRGTkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGwevaq 119
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFA--DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 120 pvqhnwktmaeaVQNHVKSLNWGhrvQLQDR---------------------KVKYFNIKASFVDEHTVRGvdkgGKATL 178
Cdd:PRK07846 66 ------------VDAELDGVRWP---DIVSRvfgridpiaaggeeyrgrdtpNIDVYRGHARFIGPKTLRT----GDGEE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 179 LSAEHIVIATGGRPRYPTQVKGA-LEYGiTSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRS-IPLRGF 256
Cdd:PRK07846 127 ITADQVVIAAGSRPVIPPVIADSgVRYH-TSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHL 205
|
250
....*....|....*
gi 15489159 257 DQQMSSLVTEHMESH 271
Cdd:PRK07846 206 DDDISERFTELASKR 220
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
37-318 |
1.01e-24 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 104.62 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 37 QQSFDLLVIGGGSGGLACAKEAAQLGKKVAVADyvEPSPRGTKWGLGGTCVNVGCIPKKlmhqaALLGG--MIRDAHH-- 112
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIE--AWKNPKGKPALGGTCLNVGCIPSK-----ALLASseEFENAGHhf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 113 --YGWEVAQpVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFV---DEHTVRGVdKGGKATLLSAEHIVIA 187
Cdd:PRK06327 75 adHGIHVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKV-TGEDETVITAKHVIIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 188 TGGRPRYPTQVKGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM--MRSIpLRGFDQQMSSLVT 265
Cdd:PRK06327 153 TGSEPRHLPGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeaLPAF-LAAADEQVAKEAA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15489159 266 EHMESHGTQFLKGCVPSHIKKLpTNQLQVTWEDhASGKEDTGTFDTVLWAIGK 318
Cdd:PRK06327 232 KAFTKQGLDIHLGVKIGEIKTG-GKGVSVAYTD-ADGEAQTLEVDKLIVSIGR 282
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
40-331 |
1.89e-23 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 100.59 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPRGtkwgLGGTCVNVGCIPKKLMHQAAllggmirdahHYGWEVAQ 119
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVAL---VEESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 120 PVQHNwktmaEAVQNHVKSLNWGhrvQLQDRKVKYFNIKASFVDEHTVRgVDKGGKATLLSAEHIVIATGGRP-RYPTQV 198
Cdd:PRK07251 67 VMATK-----NTVTSRLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIE-VQAGDEKIELTAETIVINTGAVSnVLPIPG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 199 KGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSIPLRGFDQQMSSLVTEHMESHGTQFLK 277
Cdd:PRK07251 138 LADSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLL 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 278 GCVPSHIKKlPTNQLQVTWEDhasgkeDTGTFDTVLWAIGKDAAS------HTDTVSSSR 331
Cdd:PRK07251 218 NAHTTEVKN-DGDQVLVVTED------ETYRFDALLYATGRKPNTeplgleNTDIELTER 270
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
40-266 |
8.09e-23 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 98.68 E-value: 8.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAqlGKKVAVADyvepspRGTkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGweVAQ 119
Cdd:TIGR03452 3 YDLIIIGTGSGNSIPDPRFA--DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 120 PVQH-NWKTMAEAVqnhvkslnWGHRVQL------------QDRKVKYFNIKASFVDEHTVRgvdkGGKATLLSAEHIVI 186
Cdd:TIGR03452 70 EIDSvRWPDIVSRV--------FGDRIDPiaaggedyrrgdETPNIDVYDGHARFVGPRTLR----TGDGEEITGDQIVI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 187 ATGGRPRYPTQVkgaLEYGI---TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSIP-LRGFDQQMSS 262
Cdd:TIGR03452 138 AAGSRPYIPPAI---ADSGVryhTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKlLRHLDEDISD 214
|
....
gi 15489159 263 LVTE 266
Cdd:TIGR03452 215 RFTE 218
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
2-276 |
5.79e-22 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 96.76 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 2 VAAMVAALRG----------PSRRFRPRTRALTRGTRGAA-SAAGGQQSFDLLVIGGGSGGLACAKEAAQLGKKVAVADy 70
Cdd:PRK13748 50 PDALTAAVAGlgyratladaPPTDNRGGLLDKMRGWLGGAdKHSGNERPLHVAVIGSGGAAMAAALKAVEQGARVTLIE- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 71 vepspRGTkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQPVQHNWKTMAEAVQNHVKSLnwghrvqlqdR 150
Cdd:PRK13748 129 -----RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQQARVDEL----------R 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 151 KVKYFNI------------KASFVDEHT--VRGVDKGGKAtlLSAEHIVIATGGRPRYP--TQVKGALEYgiTSDDIFWL 214
Cdd:PRK13748 191 HAKYEGIldgnpaitvlhgEARFKDDQTliVRLNDGGERV--VAFDRCLIATGASPAVPpiPGLKETPYW--TSTEALVS 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15489159 215 KESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSIPLRGFDQQMSSLVTEHMESHGTQFL 276
Cdd:PRK13748 267 DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVL 328
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
17-241 |
1.94e-16 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 80.34 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 17 RPRTRALTRGTRGAASAAG--GQQSFDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSprgtkwgLGGTCVNVGCIPK 94
Cdd:PTZ00153 92 QPRSEKSLRANGFATSQSMnfSDEEYDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDDS-------IGGTCVNVGCIPS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 95 KLMHQAALLGGMIRDAHH---YG-----------------WEVAQPVQHNWKTMAEAVQNHVKSLNWG-------HRVQL 147
Cdd:PTZ00153 165 KALLYATGKYRELKNLAKlytYGiytnafkngkndpvernQLVADTVQIDITKLKEYTQSVIDKLRGGienglksKKFCK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 148 QDRKVKYFNIKASFVDEHTVRGvDKGGKAtlLSAEHIVIATGGRPRYPTQVKGALEYGITSDDIFWLKESPGKTLVVGAS 227
Cdd:PTZ00153 245 NSEHVQVIYERGHIVDKNTIKS-EKSGKE--FKVKNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMG 321
|
250
....*....|....
gi 15489159 228 YVALECAGFLTGIG 241
Cdd:PTZ00153 322 IIGLEFMDIYTALG 335
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
220-286 |
4.66e-16 |
|
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: 72.24 E-value: 4.66e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15489159 220 KTLVVGASYVALECAGFLTGIGLDTTVM-MRSIPLRGFDQQMSSLVTEHMESHGTQFLKGCVPSHIKK 286
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEG 68
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
155-317 |
5.61e-14 |
|
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: 71.77 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 155 FNIKasFVDEHTVRGVDKGGKA------TLLSAEHIVIATGGRPRYPtQVKGALEYGITS----DDIFWLKE-----SPG 219
Cdd:COG0446 49 KGID--VRTGTEVTAIDPEAKTvtlrdgETLSYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 220 KTLVVGASYVALECAGFLTGIGLDTTVM-MRSIPLRGFDQQMSSLVTEHMESHGTQFLKGCVPSHIKklPTNQLQVTWED 298
Cdd:COG0446 126 RAVVIGGGPIGLELAEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTD 203
|
170
....*....|....*....
gi 15489159 299 hasgkEDTGTFDTVLWAIG 317
Cdd:COG0446 204 -----GEEIPADLVVVAPG 217
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
40-322 |
5.65e-14 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 72.74 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPRGtkwgLGGTCVNVGCIPKKLmhqaallggMIRDAHHYGwEVAQ 119
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVAL---IEQSNAM----YGGTCINIGCIPTKT---------LVHDAQQHT-DFVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 120 PVQHNwktmaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASFVDEHTVRgVDKGGKATLLSAEHIVIATGGRPRYP---- 195
Cdd:PRK08010 67 AIQRK-----NEVVNFLRNKNFHNLADMPN--IDVIDGQAEFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPpipg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 196 -TQVKGALEygitSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSIPLRGFDQQMSSLVTEHMESHGT 273
Cdd:PRK08010 139 iTTTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGV 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15489159 274 QFLkgcVPSHIKKLPT--NQLQVTWEDHASgkedtgTFDTVLWAIGKDAAS 322
Cdd:PRK08010 215 DII---LNAHVERISHheNQVQVHSEHAQL------AVDALLIASGRQPAT 256
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
38-247 |
3.66e-13 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 70.19 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPRGtkwgLGGTCVNVGCIP-KKLMHQAallggmirDAHHygwE 116
Cdd:NF040477 2 NHYQAIIIGFGKAGKTLAATLAKAGWRVAI---IEQSAQM----YGGTCINIGCIPtKTLVHDA--------EQHQ---D 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 117 VAQPVQHNwktmaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASFVDEHTVRgVDKGGKATLLSAEHIVIATGGRPRYPT 196
Cdd:NF040477 64 FSTAMQRK-----SSVVGFLRDKNYHNLADLDN--VDVINGRAEFIDNHTLR-VFQADGEQELRGEKIFINTGAQSVLPP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15489159 197 QVKGALEYGI-TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM 247
Cdd:NF040477 136 IPGLTTTPGVyDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIF 187
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
44-246 |
8.37e-10 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 59.87 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 44 VIGGGSGGLACAKEAAQLGKKVAVadyVEPSprgtkwGLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQPVQH 123
Cdd:PRK07845 6 IIGGGPGGYEAALVAAQLGADVTV---IERD------GLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 124 nwKTMAEAVQNHVKSLNWGH----RVQLQDRKVKYFNIKASFVDE----HTVRGVDKGGKATLLSAEHIVIATGGRPRyp 195
Cdd:PRK07845 77 --RVDLPAVNARVKALAAAQsadiRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPR-- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15489159 196 tQVKGALEYG---ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTV 246
Cdd:PRK07845 153 -ILPTAEPDGeriLTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTL 205
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
40-317 |
1.36e-09 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 58.59 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWglggTCV-NVGCIPKKLMhQAALLGGMIRDAHHYGweva 118
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATT----KEIeNYPGFPEGIS-GPELAERLREQAERFG---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 119 qpvqhnwktmAEAVQNHVKSLnwghrvqlqDRKVKYFNIkasfvdehtvrgvdKGGKATLLSAEHIVIATGGRPRYPtQV 198
Cdd:COG0492 72 ----------AEILLEEVTSV---------DKDDGPFRV--------------TTDDGTEYEAKAVIIATGAGPRKL-GL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 199 KGALE-------YGITSDDIFWlkesPGKT-LVVGASYVALECAGFLTGIGLDTTVMMRSIPLRGFDqqmsSLVTEHMES 270
Cdd:COG0492 118 PGEEEfegrgvsYCATCDGFFF----RGKDvVVVGGGDSALEEALYLTKFASKVTLIHRRDELRASK----ILVERLRAN 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15489159 271 HGTQFLKGCVPSHIKKlpTNQLQ-VTWEDHASGKEDTGTFDTVLWAIG 317
Cdd:COG0492 190 PKIEVLWNTEVTEIEG--DGRVEgVTLKNVKTGEEKELEVDGVFVAIG 235
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
163-317 |
4.97e-09 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 57.07 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 163 DEHTVRgVDKGGKatlLSAEHIVIATGGRPRYPtQVKGALEYGITS----DDIFWLKE--SPGKT-LVVGASYVALECAG 235
Cdd:COG1251 85 AARTVT-LADGET---LPYDKLVLATGSRPRVP-PIPGADLPGVFTlrtlDDADALRAalAPGKRvVVIGGGLIGLEAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 236 FLTGIGLDTTV-MMRSIPL-RGFDQQMSSLVTEHMESHGTQFLKGCVPSHIKKlptnqlqvtwEDHASGKE-DTGTF--- 309
Cdd:COG1251 160 ALRKRGLEVTVvERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG----------DDRVTGVRlADGEElpa 229
|
....*...
gi 15489159 310 DTVLWAIG 317
Cdd:COG1251 230 DLVVVAIG 237
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
41-87 |
3.17e-06 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 48.44 E-value: 3.17e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15489159 41 DLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWGLGGTCV 87
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDA 47
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
41-90 |
6.75e-05 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 44.52 E-value: 6.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15489159 41 DLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPRgtkwgLGGTCVNVG 90
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLL---VERRGF-----LGGMLTSGL 42
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
40-67 |
7.60e-05 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 44.46 E-value: 7.60e-05
10 20
....*....|....*....|....*...
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAV 67
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVAL 30
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
30-85 |
9.25e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 44.33 E-value: 9.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15489159 30 AASAAGGQQSFDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPRgtkwgLGGT 85
Cdd:PRK06134 3 SAAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIV---VEKDPV-----FGGT 50
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
40-67 |
1.09e-04 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 43.63 E-value: 1.09e-04
10 20
....*....|....*....|....*...
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAV 67
Cdd:COG3075 3 FDVVVIGGGLAGLTAAIRAAEAGLRVAI 30
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
40-78 |
3.57e-04 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 42.13 E-value: 3.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAVadyVE--PSPRGT 78
Cdd:COG1053 4 YDVVVVGSGGAGLRAALEAAEAGLKVLV---LEkvPPRGGH 41
|
|
| PLN02815 |
PLN02815 |
L-aspartate oxidase |
25-86 |
3.81e-04 |
|
L-aspartate oxidase
Pssm-ID: 215436 [Multi-domain] Cd Length: 594 Bit Score: 42.39 E-value: 3.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15489159 25 RGTRGAASAAGGQQS----FDLLVIGGGSGGLACAKEAAQLGkKVAVADYVEPSPRGTKWGLGGTC 86
Cdd:PLN02815 11 IGAERASSASRLDDEstkyFDFLVIGSGIAGLRYALEVAEYG-TVAIITKDEPHESNTNYAQGGVS 75
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
43-208 |
7.14e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 41.38 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 43 LVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPRgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDahhygwevaqpVQ 122
Cdd:COG1148 144 LVIGGGIAGMTAALELAEQGYEVYL---VEKEPE-----LGGRAAQLHKTFPGLDCPQCILEPLIAE-----------VE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 123 HNWK----TMAE--AVQNHVkslnwGH-RVQLQDRKVKYFNIKAsfvdehtvrGVdkggkatllsaehIVIATGGRPrYP 195
Cdd:COG1148 205 ANPNitvyTGAEveEVSGYV-----GNfTVTIKKGPREEIEIEV---------GA-------------IVLATGFKP-YD 256
|
170
....*....|....*...
gi 15489159 196 TQVKGALEYG-----ITS 208
Cdd:COG1148 257 PTKLGEYGYGkypnvITN 274
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
39-83 |
7.84e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 41.35 E-value: 7.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15489159 39 SFDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWGLG 83
Cdd:PRK12839 8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGG 52
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
40-67 |
1.91e-03 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 40.00 E-value: 1.91e-03
10 20
....*....|....*....|....*...
gi 15489159 40 FDLLVIGGGSGGLACAKEAAQLGKKVAV 67
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAI 28
|
|
| PLN02463 |
PLN02463 |
lycopene beta cyclase |
37-75 |
2.34e-03 |
|
lycopene beta cyclase
Pssm-ID: 178082 [Multi-domain] Cd Length: 447 Bit Score: 39.70 E-value: 2.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 15489159 37 QQSFDLLVIGGGSGGLACAKEAAQLGKKVAVADyvePSP 75
Cdd:PLN02463 26 SRVVDLVVVGGGPAGLAVAQQVSEAGLSVCCID---PSP 61
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
38-76 |
2.63e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 39.54 E-value: 2.63e-03
10 20 30
....*....|....*....|....*....|....*....
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQLGKKVAVadyVEPSPR 76
Cdd:PRK09126 2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTL---IERQPL 37
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
164-272 |
2.77e-03 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 39.25 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 164 EHTVRGVDKggKATLLSAEHI-------------VIATGGRPRYPTQVKGALE--YGITS-DDIFWLKESPGKT-----L 222
Cdd:PRK09564 76 EHEVVKVDA--KNKTITVKNLktgsifndtydklMIATGARPIIPPIKNINLEnvYTLKSmEDGLALKELLKDEeikniV 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15489159 223 VVGASYVALECAGFLTGIGLDTTVMMRS--IPLRGFDQQMSSLVTEHMESHG 272
Cdd:PRK09564 154 IIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENG 205
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
220-317 |
4.30e-03 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 39.00 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15489159 220 KTLVVGASYVALECAGFLTGIGLDTTVMMRSIP-LRGFDQQMSSLVTEHMESHGTQFLKGCVPSHIkklptNQLQVTWEd 298
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKiNKLMDADMNQPILDELDKREIPYRLNEEIDAI-----NGNEVTFK- 223
|
90
....*....|....*....
gi 15489159 299 haSGKEDtgTFDTVLWAIG 317
Cdd:PRK13512 224 --SGKVE--HYDMIIEGVG 238
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
38-69 |
4.32e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 38.73 E-value: 4.32e-03
10 20 30
....*....|....*....|....*....|..
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQLGKKVAVAD 69
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLE 32
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
31-85 |
6.10e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 38.56 E-value: 6.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15489159 31 ASAAGGQQSFDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWGLGGT 85
Cdd:PRK12843 8 LSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSAGTT 62
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
38-67 |
6.50e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 38.48 E-value: 6.50e-03
10 20 30
....*....|....*....|....*....|
gi 15489159 38 QSFDLLVIGGGSGGLACAKEAAQLGKKVAV 67
Cdd:PRK07803 7 HSYDVVVIGAGGAGLRAAIEARERGLRVAV 36
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
41-92 |
8.51e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 37.76 E-value: 8.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15489159 41 DLLVIGGGSGGLACAKEAAQLGKKVAVADyvepspRGTKWGLGGTCVNVGCI 92
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLE------RGDDPGSGASGRNAGLI 46
|
|
| |
