|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
3-304 |
2.17e-146 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 413.36 E-value: 2.17e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGGQMNNTSDIENYPGF-ETISGPDLSMKMYEPLEKFGVENIYGIVE 81
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFpEGISGPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 82 NIEDHGDFKRVLTAD-EHYDAKTIILATGAKHRLVGVSGEQEYNSRGVSYCAVCDGAFFRDQDLLVIGGGDSAVEEGIYL 160
Cdd:COG0492 81 SVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 161 TQFAKKVTIVHRRDQLRAQKILQDRAFANDKIDFIWDSVVEEIKGDDvKVRSVAIKNVKTGQVTDHDFGGIFVYVGLDPV 240
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVKTGEEKELEVDGVFVAIGLKPN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518620122 241 SSMVKDLGI-TDEAGWVITDDKMKTSRPGIFAIGDIRQKDLRQIATAVGDGAIAGQEVYNYITEH 304
Cdd:COG0492 240 TELLKGLGLeLDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
4-301 |
2.48e-137 |
|
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: 390.45 E-value: 2.48e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 4 DTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGGQMNNTSDIENYPGF-ETISGPDLSMKMYEPLEKFGVENIYGIVEN 82
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFpEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 83 IEDHGDFKRVLTAD-EHYDAKTIILATGAKHRLVGVSGEQEYNSRGVSYCAVCDGAFFRDQDLLVIGGGDSAVEEGIYLT 161
Cdd:TIGR01292 81 VDKSDRPFKVYTGDgKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 162 QFAKKVTIVHRRDQLRAQKILQDRAFANDKIDFIWDSVVEEIKGDDvKVRSVAIKNVKTGQVTDHDFGGIFVYVGLDPVS 241
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDN-KVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 242 SMVKDLGITDEAGWVITDDKMKTSRPGIFAIGDIRQKDLRQIATAVGDGAIAGQEVYNYI 301
Cdd:TIGR01292 240 ELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
2-303 |
6.72e-97 |
|
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).
Pssm-ID: 132187 [Multi-domain] Cd Length: 555 Bit Score: 296.30 E-value: 6.72e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 2 IYDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGGQMNNTSDIENYPGFETISGPDLSMKMYEPLEKFGVENIYGIVE 81
Cdd:TIGR03143 4 IYDLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQAEVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 82 NIEDHGDFKRVLTADEHYDAKTIILATGAKHRLVGVSGEQEYNSRGVSYCAVCDGAFFRDQDLLVIGGGDSAVEEGIYLT 161
Cdd:TIGR03143 84 DVDFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 162 QFAKKVTIVHRRDQLRAQKILQDRAFANDKIDFIWDSVVEEIKGDDvKVRSVAIKNVKTGQVTDHDFG------GIFVYV 235
Cdd:TIGR03143 164 RYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDD-GLRYAKFVNNVTGEITEYKAPkdagtfGVFVFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518620122 236 GLDPVSSMVKDLGITDEAGWVITDDKMKTSRPGIFAIGDIRQKDLRQIATAVGDGAIAGQEVYNYITE 303
Cdd:TIGR03143 243 GYAPSSELFKGVVELDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKE 310
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
3-294 |
6.71e-69 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 222.73 E-value: 6.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIeqgAP--GGQMNNTSDIENYPGFETISGPDLSMKMYEPLEKFGVENIYGI- 79
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIV---AErfGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQr 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 80 VENIEDHGDFKRV-LTADEHYDAKTIILATGAKHRLVGVSGEQEYNSRGVSYCAVCDGAFFRDQDLLVIGGGDSAVEEGI 158
Cdd:PRK15317 289 ASKLEPAAGLIEVeLANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAI 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 159 YLTQFAKKVTIVHRRDQLRAQKILQDRAFANDKIDFIWDSVVEEIKGDDVKVRSVAIKNVKTGQVTDHDFGGIFVYVGLD 238
Cdd:PRK15317 369 DLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLV 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 518620122 239 PVSSMVKDLGITDEAGWVITDDKMKTSRPGIFAIGDIRQKDLRQIATAVGDGAIAG 294
Cdd:PRK15317 449 PNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAA 504
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
6-301 |
8.07e-57 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 186.04 E-value: 8.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 6 LVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGGQMNNTSDIENYPGFET-ISGPDLSMKMYEPLEKFGVENIYGIVENIE 84
Cdd:PRK10262 10 LILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNdLTGPLLMERMHEHATKFETEIIFDHINKVD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 85 DHGDFKRVLTADEHYDAKTIILATGAKHRLVGVSGEQEYNSRGVSYCAVCDGAFFRDQDLLVIGGGDSAVEEGIYLTQFA 164
Cdd:PRK10262 90 LQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 165 KKVTIVHRRDQLRAQKILQDRAF---ANDKIDFIWDSVVEEIKGDDVKVRSVAIKNVK-TGQVTDHDFGGIFVYVGLDPV 240
Cdd:PRK10262 170 SEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQnSDNIESLDVAGLFVAIGHSPN 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518620122 241 SSMVKDlGITDEAGWV-----ITDDKMKTSRPGIFAIGDIRQKDLRQIATAVGDGAIAGQEVYNYI 301
Cdd:PRK10262 250 TAIFEG-QLELENGYIkvqsgIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
3-290 |
2.73e-55 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 181.36 E-value: 2.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGA--PGGQMNNTSDIENYPGFETIS--GPDLSMKMYEPLEKF--GVENI 76
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGtcPYGGCVLSKALLGAAEAPEIAslWADLYKRKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 77 YG--IVENIEDHGDFKRVLTAD---EHYDAKTIILATGAKHRLVGVSGEQEYNSRGVSYCAVCDGAFF--RDQDLLVIGG 149
Cdd:pfam07992 81 LGteVVSIDPGAKKVVLEELVDgdgETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLklLPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 150 GDSAVEEGIYLTQFAKKVTIVHRRDQL------RAQKILQDRaFANDKIDFIWDSVVEEIKGDDVKVRsvaiknVKTGQV 223
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKA-LEKNGVEVRLGTSVKEIIGDGDGVE------VILKDG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518620122 224 TDHDFGGIFVYVGLDPVSSMVKDLGI-TDEAGWVITDDKMKTSRPGIFAIGDIRQKDLRQIATAVGDG 290
Cdd:pfam07992 234 TEIDADLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
3-275 |
2.02e-27 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 110.56 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGG------------------QMNNTSDIENYpGFETiSGPDLSM-K 63
Cdd:COG1249 4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGtclnvgcipskallhaaeVAHEARHAAEF-GISA-GAPSVDWaA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 64 MYEPLEKFgVENIYGIVEN---------IEDHGDFKR----VLTADEHYDAKTIILATGAKHRLVGVSGEQEynSRGVSY 130
Cdd:COG1249 82 LMARKDKV-VDRLRGGVEEllkkngvdvIRGRARFVDphtvEVTGGETLTADHIVIATGSRPRVPPIPGLDE--VRVLTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 131 cavcDGAFFRDQ---DLLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQL------RAQKILQdRAFANDKIDFIWDSVVE 201
Cdd:COG1249 159 ----DEALELEElpkSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpgedpEISEALE-KALEKEGIDILTGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 202 EIK--GDDVKVRsVAIKNVKTGQVTDHdfggIFVYVGLDPVssmVKDLGI------TDEAGWVITDDKMKTSRPGIFAIG 273
Cdd:COG1249 234 SVEktGDGVTVT-LEDGGGEEAVEADK----VLVATGRRPN---TDGLGLeaagveLDERGGIKVDEYLRTSVPGIYAIG 305
|
..
gi 518620122 274 DI 275
Cdd:COG1249 306 DV 307
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
3-275 |
1.17e-23 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 100.25 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGG---------------------QMNNTSDIENYPGFETISGP--- 58
Cdd:PRK06292 4 YDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGtclnvgcipskaliaaaeafhEAKHAEEFGIHADGPKIDFKkvm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 59 --------DLSMKMYEPLEKF-GVENIYGIVENIEDHgdfkRVLTADEHYDAKTIILATGAkhRLVGVSGEQEYNSRG-V 128
Cdd:PRK06292 84 arvrrerdRFVGGVVEGLEKKpKIDKIKGTARFVDPN----TVEVNGERIEAKNIVIATGS--RVPPIPGVWLILGDRlL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 129 SYcavcDGAFFRD---QDLLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQL----------RAQKILQDRafandkIDFI 195
Cdd:PRK06292 158 TS----DDAFELDklpKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE------FKIK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 196 WDSVVEEIKGDDVKVRSVAIKNvktGQVTDHDFGGIFVYVGLDPVSSM--VKDLGI-TDEAGWVITDDKMKTSRPGIFAI 272
Cdd:PRK06292 228 LGAKVTSVEKSGDEKVEELEKG---GKTETIEADYVLVATGRRPNTDGlgLENTGIeLDERGRPVVDEHTQTSVPGIYAA 304
|
...
gi 518620122 273 GDI 275
Cdd:PRK06292 305 GDV 307
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
2-296 |
1.38e-19 |
|
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: 88.47 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 2 IYDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGGQMNNTSDI---------ENYPGFET-------ISGPDLSM-KM 64
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIptkallhsaEVYDEIKHakdlgieVENVSVDWeKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 65 YEPLEKF------GVENIY--GIVENIEDHGDF---KRVLTADEHYD----AKTIILATGAKHR----LVGVSGEQEYNS 125
Cdd:TIGR01350 81 QKRKNKVvkklvgGVSGLLkkNKVTVIKGEAKFldpGTVSVTGENGEetleAKNIIIATGSRPRslpgPFDFDGKVVITS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 126 rgvsycavcDGAFFRD---QDLLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQLRAQ------KILQdRAFANDKIDFIW 196
Cdd:TIGR01350 161 ---------TGALNLEevpESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGedaevsKVLQ-KALKKKGVKILT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 197 DSVVEEIKGDDvkvRSVAIKNVKTGQVT-DHDFggIFVYVGLDPVSSM--VKDLGI-TDEAGWVITDDKMKTSRPGIFAI 272
Cdd:TIGR01350 231 NTKVTAVEKND---DQVTYENKGGETETlTGEK--VLVAVGRKPNTEGlgLEKLGVeLDERGRIVVDEYMRTNVPGIYAI 305
|
330 340
....*....|....*....|....*...
gi 518620122 273 GD-IRQKDLRQIATAVGDGA---IAGQE 296
Cdd:TIGR01350 306 GDvIGGPMLAHVASHEGIVAaenIAGKE 333
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
3-275 |
5.66e-17 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 80.58 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGG---------------------QMNNTSDIENYPGFETIsgpD-- 59
Cdd:PRK06416 5 YDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGtclnrgcipskallhaaeradEARHSEDFGIKAENVGI---Dfk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 60 --------LSMKMYEPLE----KFGVENIYGiveniedHGDFK-----RVLTA--DEHYDAKTIILATGAKHR-LVG--V 117
Cdd:PRK06416 82 kvqewkngVVNRLTGGVEgllkKNKVDIIRG-------EAKLVdpntvRVMTEdgEQTYTAKNIILATGSRPReLPGieI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 118 SGEQEYNSrgvsycavcDGAFFRD---QDLLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQLRA------QKILQdRAFA 188
Cdd:PRK06416 155 DGRVIWTS---------DEALNLDevpKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPgedkeiSKLAE-RALK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 189 NDKIDFIWDSVVEEIKGDDVKVrSVAIknVKTGQVTDHDFGGIFVYVGLDPVSSMV--KDLGITDEAGWVITDDKMKTSR 266
Cdd:PRK06416 225 KRGIKIKTGAKAKKVEQTDDGV-TVTL--EDGGKEETLEADYVLVAVGRRPNTENLglEELGVKTDRGFIEVDEQLRTNV 301
|
....*....
gi 518620122 267 PGIFAIGDI 275
Cdd:PRK06416 302 PNIYAIGDI 310
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
7-305 |
1.42e-16 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 79.45 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 7 VIGSGPGGMTAALYAGRSNLKVglieqgapggqmnntsdienypgfeTIsgpdlsmkmYEPLEKFGVENIYGI------- 79
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDV-------------------------TI---------FEARDKAGGLLRYGIpefrlpk 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 80 ------VENIEDHG-DFK------RVLTADE---HYDAktIILATGA-KHRLVGVSGEqeyNSRGVsYCAV--------- 133
Cdd:PRK11749 191 divdreVERLLKLGvEIRtntevgRDITLDElraGYDA--VFIGTGAgLPRFLGIPGE---NLGGV-YSAVdfltrvnqa 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 134 -CDGAFFRDQDLLVIGGGD-------SAVEEGiyltqfAKKVTIVHRRDQ--LRAQKilQDRAFA-NDKIDFIWDSVVEE 202
Cdd:PRK11749 265 vADYDLPVGKRVVVIGGGNtamdaarTAKRLG------AESVTIVYRRGReeMPASE--EEVEHAkEEGVEFEWLAAPVE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 203 IKGDDVKVRSVAIKNVKTGqvtDHDFGG-----------------IFVYVGLDP---VSSMVKDLGITDEaGWVITDDK- 261
Cdd:PRK11749 337 ILGDEGRVTGVEFVRMELG---EPDASGrrrvpiegseftlpadlVIKAIGQTPnplILSTTPGLELNRW-GTIIADDEt 412
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 518620122 262 MKTSRPGIFAIGDI-RQKDLrqIATAVGDGAIAGQEVYNYITEHA 305
Cdd:PRK11749 413 GRTSLPGVFAGGDIvTGAAT--VVWAVGDGKDAAEAIHEYLEGAA 455
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
7-300 |
3.42e-16 |
|
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: 78.25 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 7 VIGSGPGGMTAALYAGRSnlkvglieqgapggqmnntsdienypGFE-TIsgpdlsmkmYEPLEKFGVENIYGI------ 79
Cdd:COG0493 126 VVGSGPAGLAAAYQLARA--------------------------GHEvTV---------FEALDKPGGLLRYGIpefrlp 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 80 -------VENIEDHG-DFK------RVLTADE---HYDAktIILATGA-KHRLVGVSGEqeyNSRGVsYCAVcdgAFFRD 141
Cdd:COG0493 171 kdvldreIELIEALGvEFRtnvevgKDITLDElleEFDA--VFLATGAgKPRDLGIPGE---DLKGV-HSAM---DFLTA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 142 QDL--------------LVIGGGD-------SAVEEGiyltqfAKKVTIVHRRDQLR--AQKILQDRAFAnDKIDFIWDS 198
Cdd:COG0493 242 VNLgeapdtilavgkrvVVIGGGNtamdcarTALRLG------AESVTIVYRRTREEmpASKEEVEEALE-EGVEFLFLV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 199 VVEEIKGD-DVKVRSVAIKNVKTGQVTDHDF-------GGIFVY--------VGLDPVSS-MVKDLGI-TDEAGWVITDD 260
Cdd:COG0493 315 APVEIIGDeNGRVTGLECVRMELGEPDESGRrrpvpieGSEFTLpadlvilaIGQTPDPSgLEEELGLeLDKRGTIVVDE 394
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 518620122 261 K-MKTSRPGIFAIGDIR--QKDlrqIATAVGDGAIAGQEVYNY 300
Cdd:COG0493 395 EtYQTSLPGVFAGGDAVrgPSL---VVWAIAEGRKAARAIDRY 434
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
80-273 |
4.74e-16 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 76.88 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 80 VENIEDHGDFKRVLTADEHYDAKTIILATG--AKHRLVGVSgeqEYnsrGVSYCAVCDGAFFRDQDLLVIGGGDSAVEEG 157
Cdd:pfam13738 98 VTSVKKEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVP---EL---PKHYSYVKDFHPYAGQKVVVIGGYNSAVDAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 158 IYLTQFAKKVTIVHRRDQLRAQK----------ILQ--DRAFANDKIDFIWDSVVEEIKGDDVKVRsvaIKNVKTGQVTD 225
Cdd:pfam13738 172 LELVRKGARVTVLYRGSEWEDRDsdpsyslspdTLNrlEELVKNGKIKAHFNAEVKEITEVDVSYK---VHTEDGRKVTS 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518620122 226 HDFggiFVY-VGLDP-VSSMVKDLGITDEAGW-VITDDKMKTSRPGIFAIG 273
Cdd:pfam13738 249 NDD---PILaTGYHPdLSFLKKGLFELDEDGRpVLTEETESTNVPGLFLAG 296
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
59-274 |
6.26e-16 |
|
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: 76.77 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 59 DLSMKMYEPLEKFGVENIYG-IVENIEDhgDFKRVLTAD---EHYDAktIILATGAKHRLVGVSGeqeYNSRGVSYCAVC 134
Cdd:COG0446 37 DLLVRTPESFERKGIDVRTGtEVTAIDP--EAKTVTLRDgetLSYDK--LVLATGARPRPPPIPG---LDLPGVFTLRTL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 135 DGAF--------FRDQDLLVIGGG-------DSAVEEGiyltqfaKKVTIVHRRDQL----------RAQKILQDRafan 189
Cdd:COG0446 110 DDADalrealkeFKGKRAVVIGGGpiglelaEALRKRG-------LKVTLVERAPRLlgvldpemaaLLEEELREH---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 190 dKIDFIWDSVVEEIKGDD-VKVRsvaiknVKTGQVTDHDFggIFVYVGLDPVSSMVKDLGI-TDEAGWVITDDKMKTSRP 267
Cdd:COG0446 179 -GVELRLGETVVAIDGDDkVAVT------LTDGEEIPADL--VVVAPGVRPNTELAKDAGLaLGERGWIKVDETLQTSDP 249
|
....*..
gi 518620122 268 GIFAIGD 274
Cdd:COG0446 250 DVYAAGD 256
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
144-213 |
1.44e-14 |
|
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: 67.61 E-value: 1.44e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518620122 144 LLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQLR------AQKILQDRaFANDKIDFIWDSVVEEIKGDDVKVRSV 213
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEK-LEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
3-275 |
4.61e-14 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 72.11 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGGQMNN---------------TSDIENY-PGF---ETISGPDLSmK 63
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNvgcvpkklmwygaqiAEAFHDYaPGYgfdVTENKFDWA-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 64 MYEPLEKFgVENIYGI---------VENIEDHGDF---KRVLTADEHYDAKTIILATGAKhrlvgvsgEQEYNSRGVSYC 131
Cdd:PRK06116 84 LIANRDAY-IDRLHGSyrnglenngVDLIEGFARFvdaHTVEVNGERYTADHILIATGGR--------PSIPDIPGAEYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 132 AVCDGAFFRD---QDLLVIGGGDSAVE-EGIyLTQFAKKVTIVHRRDQ-LRA-----QKILQDrAFANDKIDFIWDSVVE 201
Cdd:PRK06116 155 ITSDGFFALEelpKRVAVVGAGYIAVEfAGV-LNGLGSETHLFVRGDApLRGfdpdiRETLVE-EMEKKGIRLHTNAVPK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 202 EIKGDDVKVRSVAIKNVKTgQVTDHdfggIFVYVGLDPvssMVKDLGI------TDEAGWVITDDKMKTSRPGIFAIGDI 275
Cdd:PRK06116 233 AVEKNADGSLTLTLEDGET-LTVDC----LIWAIGREP---NTDGLGLenagvkLNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
3-278 |
1.13e-13 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 71.00 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGGQMNNT---------------SDIEN--YPGFETISGPDLSMK-- 63
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTgcvptktliasaraaHLARRaaEYGVSVGGPVSVDFKav 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 64 ---MYEPLEKF--GVENIYGIVENIE---DHGDF---KRVLTADEHYDAKTIILATGAKHRLVGVSGEQEynsrgVSYCA 132
Cdd:PRK06370 86 marKRRIRARSrhGSEQWLRGLEGVDvfrGHARFespNTVRVGGETLRAKRIFINTGARAAIPPIPGLDE-----VGYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 133 vCDGAF---FRDQDLLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQL------RAQKILQDrAFANDKIDFIWDSVVEEI 203
Cdd:PRK06370 161 -NETIFsldELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLlpredeDVAAAVRE-ILEREGIDVRLNAECIRV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 204 KGDDVKVRSVAIKNVKTGQVT-DHdfggIFVYVGLDPvssMVKDLGI------TDEAGWVITDDKMKTSRPGIFAIGDIR 276
Cdd:PRK06370 239 ERDGDGIAVGLDCNGGAPEITgSH----ILVAVGRVP---NTDDLGLeaagveTDARGYIKVDDQLRTTNPGIYAAGDCN 311
|
..
gi 518620122 277 QK 278
Cdd:PRK06370 312 GR 313
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
1-304 |
3.11e-12 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 66.95 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 1 MIYDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGG-----------------QMNNTSDIENYPGFETISGPDLSM- 62
Cdd:PTZ00058 47 MVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGtcvnvgcvpkkimfnaaSIHDILENSRHYGFDTQFSFNLPLl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 63 ------------KMYEP-LEKFGVENIYGIVENI-EDHGDFKRVLTADEHYDA----KTIILATG-----------AKHR 113
Cdd:PTZ00058 127 verrdkyirrlnDIYRQnLKKDNVEYFEGKGSLLsENQVLIKKVSQVDGEADEsdddEVTIVSAGvsqlddgqvieGKNI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 114 LVGVSGEQEY-NSRGVSYCAVCDGaFFRDQD---LLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQLRaqkilqdRAFAN 189
Cdd:PTZ00058 207 LIAVGNKPIFpDVKGKEFTISSDD-FFKIKEakrIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL-------RKFDE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 190 DKID------------FIWDSVVEEIKgddvKVRSVAIKNVKTGQVTDHDFGGIFVYVGLDPVSSMV--KDLGITDEAGW 255
Cdd:PTZ00058 279 TIINelendmkknninIITHANVEEIE----KVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLnlKALNIKTPKGY 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 518620122 256 VITDDKMKTSRPGIFAIGDIRQKDLRQIATAVGDGAIAGQEVYNYITEH 304
Cdd:PTZ00058 355 IKVDDNQRTSVKHIYAVGDCCMVKKNQEIEDLNLLKLYNEEPYLKKKEN 403
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
6-275 |
1.97e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 64.00 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 6 LVIGSGPGGMTAALYAGR---SNLKVGLIEQ-----------GAPGGQMNnTSDIEnypgfetisgPDLSmkmyEPLEKF 71
Cdd:COG1252 5 VIVGGGFAGLEAARRLRKklgGDAEVTLIDPnpyhlfqpllpEVAAGTLS-PDDIA----------IPLR----ELLRRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 72 GVENIYGIVENIeDHGDfKRVLTAD---EHYDakTIILATGAKHRLVGVSGEQEYnsrGVSYCAVCDGAFFRDQ------ 142
Cdd:COG1252 70 GVRFIQGEVTGI-DPEA-RTVTLADgrtLSYD--YLVIATGSVTNFFGIPGLAEH---ALPLKTLEDALALRERllaafe 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 143 -----DLL---VIGGGDSAVE---------------EGIYLTQFakKVTIVHRRDQL----------RAQKILQDRafan 189
Cdd:COG1252 143 raerrRLLtivVVGGGPTGVElagelaellrkllryPGIDPDKV--RITLVEAGPRIlpglgeklseAAEKELEKR---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 190 dKIDFIWDSVVEEIKGDDVKVrsvaiknvKTGQVTDHDFggIFVYVGLDPvSSMVKDLGI-TDEAGWVITDDKMKTSR-P 267
Cdd:COG1252 217 -GVEVHTGTRVTEVDADGVTL--------EDGEEIPADT--VIWAAGVKA-PPLLADLGLpTDRRGRVLVDPTLQVPGhP 284
|
....*...
gi 518620122 268 GIFAIGDI 275
Cdd:COG1252 285 NVFAIGDC 292
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
90-275 |
1.13e-10 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 61.70 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 90 KRVLTAD---EHYDAktIILATGAKHRLVGVSGEqeyNSRGVSYcavcdgafFRDQD--------------LLVIGGG-- 150
Cdd:COG1251 87 RTVTLADgetLPYDK--LVLATGSRPRVPPIPGA---DLPGVFT--------LRTLDdadalraalapgkrVVVIGGGli 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 151 -----DSAVEEGIyltqfakKVTIVHRRDQL-------RAQKILQdRAFANDKIDFIWDSVVEEIKGDDvKVRSVAIKNv 218
Cdd:COG1251 154 gleaaAALRKRGL-------EVTVVERAPRLlprqldeEAGALLQ-RLLEALGVEVRLGTGVTEIEGDD-RVTGVRLAD- 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518620122 219 ktGQVTDHDFggIFVYVGLDPVSSMVKDLGITDEAGwVITDDKMKTSRPGIFAIGDI 275
Cdd:COG1251 224 --GEELPADL--VVVAIGVRPNTELARAAGLAVDRG-IVVDDYLRTSDPDIYAAGDC 275
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
7-304 |
1.55e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 61.16 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 7 VIGSGPGGMTAALYAGRSNLKVGLIE-QGAPGGQMnntsdIENYPGFEtISGPDLSMKMYEpLEKFGVE-----NIYGIV 80
Cdd:PRK12770 23 IIGAGPAGLAAAGYLACLGYEVHVYDkLPEPGGLM-----LFGIPEFR-IPIERVREGVKE-LEEAGVVfhtrtKVCCGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 81 ENIEDHGD--FKRVLTADE---HYDAktIILATGA-KHRLVGVSGEQ--------EY--NSRGVSYC-----AVCDgafF 139
Cdd:PRK12770 96 PLHEEEGDefVERIVSLEElvkKYDA--VLIATGTwKSRKLGIPGEDlpgvysalEYlfRIRAAKLGylpweKVPP---V 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 140 RDQDLLVIGGGDSAVEEGI-YLTQFAKKVTIVHRRDQLRAQ------KILQDRAfandkIDFIWDSVVEEIKGDDvKVRS 212
Cdd:PRK12770 171 EGKKVVVVGAGLTAVDAALeAVLLGAEKVYLAYRRTINEAPagkyeiERLIARG-----VEFLELVTPVRIIGEG-RVEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 213 VAIKNVKTGQ-----------VTDHDFGGIFVYV----GLDPVSSMVKD-LGI-TDEAGWVITDDKMKTSRPGIFAIGDI 275
Cdd:PRK12770 245 VELAKMRLGEpdesgrprpvpIPGSEFVLEADTVvfaiGEIPTPPFAKEcLGIeLNRKGEIVVDEKHMTSREGVFAAGDV 324
|
330 340
....*....|....*....|....*....
gi 518620122 276 RQKDlRQIATAVGDGAIAGQEVYNYITEH 304
Cdd:PRK12770 325 VTGP-SKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
3-298 |
1.30e-09 |
|
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: 58.71 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAP---------GGQMNNTSDIENypgfETISGPDLSMKMYEPLEKFG- 72
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgiGGTCVNVGCIPK----KLMHQAALLGQALKDSRNYGw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 73 -VENIYG-----IVENIEDH-----------------------GDF--KRVLTA------DEHYDAKTIILATGAKHRLV 115
Cdd:TIGR01438 79 kVEETVKhdwkrLVEAVQNHigslnwgyrvalrekkvkyenayAEFvdKHRIKAtnkkgkEKIYSAERFLIATGERPRYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 116 GVSGEQEYnsrgvsyCAVCDGAFFRDQD---LLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQLRAQkilqDRAFANDKI 192
Cdd:TIGR01438 159 GIPGAKEL-------CITSDDLFSLPYCpgkTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGF----DQDCANKVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 193 DFIWDSVVEEIKGDDVKvRSVAIKNVKTGQVTDHDFGGIFVY------VGLDPVssmVKDLG-------ITDEAGWVITD 259
Cdd:TIGR01438 228 EHMEEHGVKFKRQFVPI-KVEQIEAKVLVEFTDSTNGIEEEYdtvllaIGRDAC---TRKLNlenvgvkINKKTGKIPAD 303
|
330 340 350
....*....|....*....|....*....|....*....
gi 518620122 260 DKMKTSRPGIFAIGDIRQKDLRQIATAVGDGAIAGQEVY 298
Cdd:TIGR01438 304 EEEQTNVPYIYAVGDILEDKPELTPVAIQAGRLLAQRLF 342
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
3-275 |
2.57e-09 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 57.86 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQG-APGGQMNNTSDI---------------------ENYPGFETISGPDL 60
Cdd:PRK05249 6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYrNVGGGCTHTGTIpskalreavlrligfnqnplySSYRVKLRITFADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 61 SMK-----------MYEPLEKFGVENIYGI--------VEnIEDHGDFKRVLTADehydakTIILATGAKhrlvgvsgeq 121
Cdd:PRK05249 86 LARadhvinkqvevRRGQYERNRVDLIQGRarfvdphtVE-VECPDGEVETLTAD------KIVIATGSR---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 122 EYNSRGVSYcavcDGAFFRDQD-----------LLVIGGGDSAVEegiYLTQFAK---KVTIVHRRDQLRA---QKILQD 184
Cdd:PRK05249 149 PYRPPDVDF----DHPRIYDSDsilsldhlprsLIIYGAGVIGCE---YASIFAAlgvKVTLINTRDRLLSfldDEISDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 185 --RAFANDKIDFIWDSVVEEIKGDDVKVrsvaIKNVKTGQVTDHDfgGIFVYVGLdpvSSMVKDLGI------TDEAGWV 256
Cdd:PRK05249 222 lsYHLRDSGVTIRHNEEVEKVEGGDDGV----IVHLKSGKKIKAD--CLLYANGR---TGNTDGLNLenagleADSRGQL 292
|
330
....*....|....*....
gi 518620122 257 ITDDKMKTSRPGIFAIGDI 275
Cdd:PRK05249 293 KVNENYQTAVPHIYAVGDV 311
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
7-173 |
2.61e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 57.82 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 7 VIGSGPGGMTAALYAGRSNLKVGLIEQG-APGGQMNntsdiENYPGF---ETISGPDLsmkmyEPLEKFGVENIYGIVen 82
Cdd:PRK12814 198 IIGAGPAGLTAAYYLLRKGHDVTIFDANeQAGGMMR-----YGIPRFrlpESVIDADI-----APLRAMGAEFRFNTV-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 83 iedhgdFKRVLTADE---HYDAktIILATGA-KHRLVGVSGEQeynSRGVsycaVCDGAFFRD----------QDLLVIG 148
Cdd:PRK12814 266 ------FGRDITLEElqkEFDA--VLLAVGAqKASKMGIPGEE---LPGV----ISGIDFLRNvalgtalhpgKKVVVIG 330
|
170 180
....*....|....*....|....*.
gi 518620122 149 GGDSAVEEG-IYLTQFAKKVTIVHRR 173
Cdd:PRK12814 331 GGNTAIDAArTALRLGAESVTILYRR 356
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
6-293 |
4.64e-09 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 57.19 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 6 LVIGSGPGGMTAALYAGRSNLKVGLIEQGA-PGGQMNntsdienY--PGF-----------ETIsgpdLSMkmyeplekf 71
Cdd:PRK12771 141 AVIGGGPAGLSAAYHLRRMGHAVTIFEAGPkLGGMMR-------YgiPAYrlprevldaeiQRI----LDL--------- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 72 GVENIYG--IVENIEdhgdFKRVltaDEHYDAktIILATGA-KHRLVGVSGEqeyNSRGVsYCAVcdgAFFR-----DQD 143
Cdd:PRK12771 201 GVEVRLGvrVGEDIT----LEQL---EGEFDA--VFVAIGAqLGKRLPIPGE---DAAGV-LDAV---DFLRavgegEPP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 144 LL-----VIGGGD-------SAVEEGiyltqfAKKVTIVHRR--DQLRAQKILQDRAFAnDKIDFIWDSVVEEIKGDDVK 209
Cdd:PRK12771 265 FLgkrvvVIGGGNtamdaarTARRLG------AEEVTIVYRRtrEDMPAHDEEIEEALR-EGVEINWLRTPVEIEGDENG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 210 VRSVAIKNVKTGQVTDHDF----GGIFVYVGLDPV---------SSMVKDL-GITDEAGWVITDDK-MKTSRPGIFAIGD 274
Cdd:PRK12771 338 ATGLRVITVEKMELDEDGRpspvTGEEETLEADLVvlaigqdidSAGLESVpGVEVGRGVVQVDPNfMMTGRPGVFAGGD 417
|
330
....*....|....*....
gi 518620122 275 IrQKDLRQIATAVGDGAIA 293
Cdd:PRK12771 418 M-VPGPRTVTTAIGHGKKA 435
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
7-302 |
1.65e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 55.41 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 7 VIGSGPGGMTAALYAGRSNLKVGLIEQ-GAPGGQMnntsdIENYPGF----ETISGPDLsmkmyEPLEKFGVE----NIY 77
Cdd:PRK12831 145 VIGSGPAGLTCAGDLAKMGYDVTIFEAlHEPGGVL-----VYGIPEFrlpkETVVKKEI-----ENIKKLGVKietnVVV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 78 GIVENIEDhgdfkrvLTADEHYDAktIILATGAK-HRLVGVSGEQ--------EYNSR---GVSYCAVCDGAFFRDQDLL 145
Cdd:PRK12831 215 GKTVTIDE-------LLEEEGFDA--VFIGSGAGlPKFMGIPGENlngvfsanEFLTRvnlMKAYKPEYDTPIKVGKKVA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 146 VIGGGDSAVEEGIYLTQFAKKVTIVHRR--DQLRAQKILQDRAfANDKIDFIWDSVVEEIKGDD---VKvrsvAIKNVK- 219
Cdd:PRK12831 286 VVGGGNVAMDAARTALRLGAEVHIVYRRseEELPARVEEVHHA-KEEGVIFDLLTNPVEILGDEngwVK----GMKCIKm 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 220 ----------------TGQVTDHDFGGIFVYVGLDP---VSSMVKDLGITDEAGWVITDDKMKTSRPGIFAIGDIrqkdL 280
Cdd:PRK12831 361 elgepdasgrrrpveiEGSEFVLEVDTVIMSLGTSPnplISSTTKGLKINKRGCIVADEETGLTSKEGVFAGGDA----V 436
|
330 340
....*....|....*....|....*
gi 518620122 281 RQIAT---AVGDGAIAGQEVYNYIT 302
Cdd:PRK12831 437 TGAATvilAMGAGKKAAKAIDEYLS 461
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
3-275 |
5.47e-08 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 53.78 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIE-------QGAPGGQMNNTSDI---------ENYP----GFET--ISGPDL 60
Cdd:PRK06327 5 FDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCIpskallassEEFEnaghHFADhgIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 61 SM---KMYEPLEKFGVENIYGI--------VENIEDHGDFK---------RVLTADEH-YDAKTIILATGAKHR-LVGVS 118
Cdd:PRK06327 85 KIdvaKMIARKDKVVKKMTGGIeglfkknkITVLKGRGSFVgktdagyeiKVTGEDETvITAKHVIIATGSEPRhLPGVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 119 geqeynsrgVSYCAVCD--GAFFRDQ---DLLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQLRA---QKILQD--RAFA 188
Cdd:PRK06327 165 ---------FDNKIILDntGALNFTEvpkKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAaadEQVAKEaaKAFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 189 NDKIDFIWDSVVEEIKGDDVKVrSVAIKNVKTGQVTdHDFGGIFVYVGLDPVSsmvKDLG------ITDEAGWVITDDKM 262
Cdd:PRK06327 236 KQGLDIHLGVKIGEIKTGGKGV-SVAYTDADGEAQT-LEVDKLIVSIGRVPNT---DGLGleavglKLDERGFIPVDDHC 310
|
330
....*....|...
gi 518620122 263 KTSRPGIFAIGDI 275
Cdd:PRK06327 311 RTNVPNVYAIGDV 323
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
3-275 |
1.20e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 52.44 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAP--GGQMNNTSDI---------ENYPGFE-------TISGpDLSMKM 64
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIptktllvaaEKNLSFEqvmatknTVTS-RLRGKN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 65 YEPLEKFGVENIYG---IVEN--IE-DHGDFKRVLTADehydakTIILATGAKHRLVGVSGEQE----YNSRGVSYCAVc 134
Cdd:PRK07251 83 YAMLAGSGVDLYDAeahFVSNkvIEvQAGDEKIELTAE------TIVINTGAVSNVLPIPGLADskhvYDSTGIQSLET- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 135 dgaffRDQDLLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQL--RAQKILQDRA---FANDKIDFIWDSVVEEIKGDDVK 209
Cdd:PRK07251 156 -----LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTIlpREEPSVAALAkqyMEEDGITFLLNAHTTEVKNDGDQ 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518620122 210 VrsvaiknVKTGQVTDHDFGGIFVYVGLDPvssMVKDLGI------TDEAGWVITDDKMKTSRPGIFAIGDI 275
Cdd:PRK07251 231 V-------LVVTEDETYRFDALLYATGRKP---NTEPLGLentdieLTERGAIKVDDYCQTSVPGVFAVGDV 292
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
98-275 |
6.85e-07 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 50.31 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 98 HYDakTIILATGAKHR---LVGVSGEQEYNSRGVSYCAVCDGAFFRDQDLLVIGGGDSAVEEGIYLTQFAKKVTIVHRRD 174
Cdd:PRK09754 100 HWD--QLFIATGAAARplpLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 175 QLR---AQKILQDRAFANDK---IDFIWDSVVEEI-KGDDVKVRsvaiknVKTGQVTDHDfggIFVY-VGLDPVSSMVKD 246
Cdd:PRK09754 178 TVMgrnAPPPVQRYLLQRHQqagVRILLNNAIEHVvDGEKVELT------LQSGETLQAD---VVIYgIGISANDQLARE 248
|
170 180
....*....|....*....|....*....
gi 518620122 247 LGITDEAGWVItDDKMKTSRPGIFAIGDI 275
Cdd:PRK09754 249 ANLDTANGIVI-DEACRTCDPAIFAGGDV 276
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
7-303 |
1.01e-06 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 50.13 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 7 VIGSGPGGMTAALYAGRSNLKVGLIEQ-GAPGGQM----------NNTSDIEnypgfetisgpdlsmkmYEPLEKFGVE- 74
Cdd:PRK12778 436 VIGSGPAGLSFAGDLAKRGYDVTVFEAlHEIGGVLkygipefrlpKKIVDVE-----------------IENLKKLGVKf 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 75 ---NIYGIVENIEDHGDfkrvltadEHYDAktIILATGAK-HRLVGVSGEqeyNSRGV--------------SYCAVCDG 136
Cdd:PRK12778 499 etdVIVGKTITIEELEE--------EGFKG--IFIASGAGlPNFMNIPGE---NSNGVmssneyltrvnlmdAASPDSDT 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 137 AFFRDQDLLVIGGGDSAVEEG-IYLTQFAKKVTIVHRRDQLRAQKILQDRAFANDK-IDFIWDSVVEEIKGD-DVKVRSV 213
Cdd:PRK12778 566 PIKFGKKVAVVGGGNTAMDSArTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEEgIEFLTLHNPIEYLADeKGWVKQV 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 214 AIKNVK---------------TGQVTDHDFGGIFVYVGLDP---VSSMVKDLGItDEAGWVITDDKMKTSRPGIFAIGDI 275
Cdd:PRK12778 646 VLQKMElgepdasgrrrpvaiPGSTFTVDVDLVIVSVGVSPnplVPSSIPGLEL-NRKGTIVVDEEMQSSIPGIYAGGDI 724
|
330 340 350
....*....|....*....|....*....|.
gi 518620122 276 rqkdLRQIAT---AVGDGAIAGQEVYNYITE 303
Cdd:PRK12778 725 ----VRGGATvilAMGDGKRAAAAIDEYLSS 751
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
94-283 |
1.35e-06 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 49.40 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 94 TADEHYDakTIILATGAKHRLVGVSGEQEYNSRGVSYCAVCDGAFFRDQ--DLLVIGGGDSAVEEGIYLTQFAKKVTIVH 171
Cdd:PRK13512 101 QFEESYD--KLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQvdKALVVGAGYISLEVLENLYERGLHPTLIH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 172 RR-------DQLRAQKILQDraFANDKIDFIWDSVVEEIKGDDVkvrsvaikNVKTGQVTDHDFggIFVYVGLDPVSSMV 244
Cdd:PRK13512 179 RSdkinklmDADMNQPILDE--LDKREIPYRLNEEIDAINGNEV--------TFKSGKVEHYDM--IIEGVGTHPNSKFI 246
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518620122 245 KDLGIT-DEAGWVITDDKMKTSRPGIFAIGDIRQKDLRQI 283
Cdd:PRK13512 247 ESSNIKlDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-38 |
1.90e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.08 E-value: 1.90e-06
10 20 30
....*....|....*....|....*....|....*....
gi 518620122 1 MIYDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGA-PGG 38
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDtPGG 40
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
3-140 |
3.63e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 47.96 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQG---------APGGQMN--NTSD-----IENYPGfetisGPDlsmKMYE 66
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGkklgrkiliSGGGRCNvtNLSEepdnfLSRYPG-----NPK---FLKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 67 PLEKFGVENI------YGIVENIEDHGdfkRVLTADEhyDAKTIILATGAKHRLVGVsgEQEYNSRgVSYCAVCDGAFFR 140
Cdd:pfam03486 73 ALSRFTPWDFiaffesLGVPLKEEDHG---RLFPDSD--KASDIVDALLNELKELGV--KIRLRTR-VLSVEKDDDGRFR 144
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
6-112 |
4.72e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 47.93 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 6 LVIGSGPGGMTAALYAGRSNLKVGLIE-QGAPGGQMNNTsdienypgFETISGPDLSMKMYEPLEKfGVE---NI----Y 77
Cdd:COG1148 144 LVIGGGIAGMTAALELAEQGYEVYLVEkEPELGGRAAQL--------HKTFPGLDCPQCILEPLIA-EVEanpNItvytG 214
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 518620122 78 GIVENIEDH-GDF------KRVLTADEHYDAktIILATGAKH 112
Cdd:COG1148 215 AEVEEVSGYvGNFtvtikkGPREEIEIEVGA--IVLATGFKP 254
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
3-38 |
1.17e-05 |
|
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: 46.36 E-value: 1.17e-05
10 20 30
....*....|....*....|....*....|....*.
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGG 38
Cdd:COG1053 4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
3-275 |
2.29e-05 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 45.39 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAP--GGQMNN---------TSDIENYPGFETISGPD------LSMKMY 65
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAmyGGTCINigciptktlVHDAQQHTDFVRAIQRKnevvnfLRNKNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 66 EPLEKF-GVENIYGIVENIEDHGdfKRVLTADEHYD--AKTIILATGAKHRLVGVSGEQE----YNSRGVSYCAVcdgaf 138
Cdd:PRK08010 84 HNLADMpNIDVIDGQAEFINNHS--LRVHRPEGNLEihGEKIFINTGAQTVVPPIPGITTtpgvYDSTGLLNLKE----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 139 fRDQDLLVIGGGDSAVEEGIYLTQFAKKVTIVH-------RRDQLRAQ---KILQDRAfandkIDFIWDSVVEEIKGDDV 208
Cdd:PRK08010 157 -LPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslflpREDRDIADniaTILRDQG-----VDIILNAHVERISHHEN 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 209 KVRsvaiknVKTGQvTDHDFGGIFVYVGLDPVSSMV--KDLGI-TDEAGWVITDDKMKTSRPGIFAIGDI 275
Cdd:PRK08010 231 QVQ------VHSEH-AQLAVDALLIASGRQPATASLhpENAGIaVNERGAIVVDKYLHTTADNIWAMGDV 293
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
3-229 |
3.70e-05 |
|
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: 44.85 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGA-PGGqmnnTSDIENYPGFETISGPDLS----MKMYEPLEKF------ 71
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADdVGG----TWRDNRYPGLRLDTPSHLYslpfFPNWSDDPDFptgdei 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 72 -----GVENIYGIVENI------------EDHGDFkRVLTAD-EHYDAKTIILATGAKHR-----LVGV---SGEQ---- 121
Cdd:COG2072 83 layleAYADKFGLRRPIrfgtevtsarwdEADGRW-TVTTDDgETLTARFVVVATGPLSRpkipdIPGLedfAGEQlhsa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 122 EYNsrgvsycavcDGAFFRDQDLLVIGGGDSAVEEGIYLTQFAKKVTIVhrrdQLRAQKILQDRAFANDKIDFIWDSVVE 201
Cdd:COG2072 162 DWR----------NPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVF----QRTPPWVLPRPNYDPERGRPANYLGLE 227
|
250 260
....*....|....*....|....*....
gi 518620122 202 -EIKGDDVKVRSVAIKNVKtGQVTDHDFG 229
Cdd:COG2072 228 aPPALNRRDARAWLRRLLR-AQVKDPELG 255
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
7-300 |
5.37e-05 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 44.38 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 7 VIGSGPGGMTAALYAGRSNLKV----------GLIEQGAPggqmnntsdienypgfetisgpdlSMKM--------YEPL 68
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVtvferadrigGLLRYGIP------------------------DFKLekevidrrIELM 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 69 EKFGVENIYGIveNIedhGdfkRVLTADE---HYDAktIILATGA-KHRLVGVSGEQeynSRGVsYCAV----------- 133
Cdd:PRK12810 204 EAEGIEFRTNV--EV---G---KDITAEEllaEYDA--VFLGTGAyKPRDLGIPGRD---LDGV-HFAMdfliqntrrvl 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 134 --CDGAFFR--DQDLLVIGGGDSAVE-EGIYLTQFAKKVTivhRRDQ-----LRAQKILQDRAFANDK---------IDF 194
Cdd:PRK12810 270 gdETEPFISakGKHVVVIGGGDTGMDcVGTAIRQGAKSVT---QRDImpmppSRRNKNNPWPYWPMKLevsnaheegVER 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 195 IWDSVVEEIKGDDVKVRsvAIKNVKTgQVTDHDF----GGIFV-----------YVGldPVSSMVKDLGI-TDEAGWVIT 258
Cdd:PRK12810 347 EFNVQTKEFEGENGKVT--GVKVVRT-ELGEGDFepveGSEFVlpadlvllamgFTG--PEAGLLAQFGVeLDERGRVAA 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 518620122 259 DD-KMKTSRPGIFAIGDIRQ-KDLrqIATAVGDGAIAGQEVYNY 300
Cdd:PRK12810 422 PDnAYQTSNPKVFAAGDMRRgQSL--VVWAIAEGRQAARAIDAY 463
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
3-32 |
7.28e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 43.96 E-value: 7.28e-05
10 20 30
....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIE 32
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVE 46
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
4-40 |
8.31e-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: 43.75 E-value: 8.31e-05
10 20 30
....*....|....*....|....*....|....*...
gi 518620122 4 DTLVIGSGPGGMTAALYAGRSNLKVGLIEQ-GAPGGQM 40
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERrGFLGGML 38
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
4-38 |
1.63e-04 |
|
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: 42.66 E-value: 1.63e-04
10 20 30
....*....|....*....|....*....|....*
gi 518620122 4 DTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGG 38
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFG 35
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
3-35 |
2.54e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 42.49 E-value: 2.54e-04
10 20 30
....*....|....*....|....*....|...
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGA 35
Cdd:PRK12835 12 VDVLVVGSGGGGMTAALTAAARGLDTLVVEKSA 44
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
3-275 |
2.83e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 42.12 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAP---------GGQMNNTS-------------------DIENYpGFET 54
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPstqgtkwglGGTCVNVGcvpkklmhyaanigsifhhDSQMY-GWKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 55 ISGPD--------------LSMKMYEPLEKFGVENIYGIVENIEDHGDFKRVLTADEHYDAKTIILATGAK-HRLVGVSG 119
Cdd:PTZ00052 85 SSSFNwgklvttvqnhirsLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQEETITAKYILIATGGRpSIPEDVPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 120 EQEYNsrgvsycAVCDGAFFRDQD---LLVIGGGDSAVEEGIYLTQFAKKVTIVHRRDQLR------AQKIL-----QDR 185
Cdd:PTZ00052 165 AKEYS-------ITSDDIFSLSKDpgkTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRgfdrqcSEKVVeymkeQGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 186 AFANDKIDFIWDSVVEEIKgddvkvrsvaiknVKTGQVTDHDFGGIFVYVGLDPVSSMVK----DLGITDEAGWVITDDk 261
Cdd:PTZ00052 238 LFLEGVVPINIEKMDDKIK-------------VLFSDGTTELFDTVLYATGRKPDIKGLNlnaiGVHVNKSNKIIAPND- 303
|
330
....*....|....
gi 518620122 262 mKTSRPGIFAIGDI 275
Cdd:PTZ00052 304 -CTNIPNIFAVGDV 316
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
3-38 |
2.96e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 41.92 E-value: 2.96e-04
10 20 30
....*....|....*....|....*....|....*.
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGG 38
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
97-291 |
3.48e-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: 41.88 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 97 EHYDAKTIILATGAKHRLVGVSGeqeynsrgVSYCAVCDGAFFRDQD---LLVIGGGDSAVE-EGIYLTQFAK--KVTIV 170
Cdd:TIGR01423 148 ERLQAEHILLATGSWPQMLGIPG--------IEHCISSNEAFYLDEPprrVLTVGGGFISVEfAGIFNAYKPRggKVTLC 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 171 HRRD--------QLRAQKILQDRAfanDKIDFIWDSVVEEIKGDDVKVRSVAIKnvkTGQVTDHDFggIFVYVGLDPVSS 242
Cdd:TIGR01423 220 YRNNmilrgfdsTLRKELTKQLRA---NGINIMTNENPAKVTLNADGSKHVTFE---SGKTLDVDV--VMMAIGRVPRTQ 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518620122 243 MVK----DLGITDEAGwVITDDKMKTSRPGIFAIGDIRQKdLRQIATAVGDGA 291
Cdd:TIGR01423 292 TLQldkvGVELTKKGA-IQVDEFSRTNVPNIYAIGDVTDR-VMLTPVAINEGA 342
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
3-35 |
7.18e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 41.17 E-value: 7.18e-04
10 20 30
....*....|....*....|....*....|...
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGA 35
Cdd:PRK07843 8 YDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAP 40
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
1-34 |
1.20e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 40.22 E-value: 1.20e-03
10 20 30
....*....|....*....|....*....|....
gi 518620122 1 MIYDTLVIGSGPGGMTAALYAGRSNLKVGLIEQG 34
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKG 34
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
7-40 |
1.30e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 36.74 E-value: 1.30e-03
10 20 30
....*....|....*....|....*....|....*
gi 518620122 7 VIGSGPGGMTAALYAGRSNLKVGLIEQGA-PGGQM 40
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDrLGGNA 35
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
3-38 |
1.50e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.89 E-value: 1.50e-03
10 20 30
....*....|....*....|....*....|....*.
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAPGG 38
Cdd:COG0665 3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
3-33 |
1.89e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 39.70 E-value: 1.89e-03
10 20 30
....*....|....*....|....*....|.
gi 518620122 3 YDTLVIGSGPGGMTAALYAGRSNLKVGLIEQ 33
Cdd:PRK06134 13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEK 43
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
1-34 |
1.92e-03 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 39.39 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....
gi 518620122 1 MIYDTLVIGSGPGGMTAALYAGRSNLKVGLIEQG 34
Cdd:COG3075 1 MKFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAG 34
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-36 |
4.21e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 38.38 E-value: 4.21e-03
10 20 30
....*....|....*....|....*....|....*.
gi 518620122 1 MIYDTLVIGSGPGGMTAALYAGRSNLKVGLIEQGAP 36
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPP 37
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
5-274 |
4.30e-03 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 38.48 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 5 TLVIGSGPGGMTAALYAGRSN--LKVGLIEQ---------GAP---GGQMNNTSD-IENYPgfETISGPDLSMKMYEPLE 69
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNkeLEITVYEKtdivsfgacGLPyfvGGFFDDPNTmIARTP--EEFIKSGIDVKTEHEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 70 KFGVENIYGIVENIEDHGDFkrvltaDEHYDakTIILATGAKHRLVGVSGEQEYNSRGVSYCAvcDGAFFRD-------Q 142
Cdd:PRK09564 81 KVDAKNKTITVKNLKTGSIF------NDTYD--KLMIATGARPIIPPIKNINLENVYTLKSME--DGLALKEllkdeeiK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518620122 143 DLLVIGGGDSAVEEGIYLTQFAKKVTIVHrrdqlRAQKILQDrAFANDkidfIWDSVVEEIKGDDV------KVRSVAIK 216
Cdd:PRK09564 151 NIVIIGAGFIGLEAVEAAKHLGKNVRIIQ-----LEDRILPD-SFDKE----ITDVMEEELRENGVelhlneFVKSLIGE 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518620122 217 NVKTGQVTDH---DFGGIFVYVGLDPVSSMVKDLGI-TDEAGWVITDDKMKTSRPGIFAIGD 274
Cdd:PRK09564 221 DKVEGVVTDKgeyEADVVIVATGVKPNTEFLEDTGLkTLKNGAIIVDEYGETSIENIYAAGD 282
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
4-40 |
5.53e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 37.45 E-value: 5.53e-03
10 20 30
....*....|....*....|....*....|....*....
gi 518620122 4 DTLVIGSGPGGMTAALY-AGRSNLKVGLIEQG-APGGQM 40
Cdd:pfam01946 19 DVVIVGAGSSGLTAAYYlAKNRGLKVAIIERSvSPGGGA 57
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
1-33 |
6.17e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 38.00 E-value: 6.17e-03
10 20 30
....*....|....*....|....*....|...
gi 518620122 1 MIYDTLVIGSGPGGMTAALYAGRSNLKVGLIEQ 33
Cdd:PRK09126 2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| |
