|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
4-305 |
1.75e-150 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 423.76 E-value: 1.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNTAEVENYPGFP-SIMGPDLGEKMYKSATKQGVEFVYGDVQ 82
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPeGISGPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 83 KIELDGQKRIVKMD-PEDITAKAVIIATGSTNRKLGIPGEEEYSGRGVSYCAVCDGAFFKDENVAVVGGGDSAISEGLYL 161
Cdd:COG0492 81 SVDKDDGPFRVTTDdGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 162 ANLAKDVDVIHRRDQLRAERVLQTRAFKNPKMEFTWDSVPVEIIGDEnKVTGVKVHNKKTDEDKVIDASGVFIYIGNVPN 241
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVKTGEEKELEVDGVFVAIGLKPN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489725795 242 SEPFKELKI-TDDQGWIITNDQMETTVPGIYAVGDVRQKKLRQIVTAVGDGGIAGQNAFEYISEL 305
Cdd:COG0492 240 TELLKGLGLeLDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
5-302 |
2.87e-138 |
|
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: 392.76 E-value: 2.87e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 5 DLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNTAEVENYPGFPS-IMGPDLGEKMYKSATKQGVEFVYGDVQK 83
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEgISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 84 IELDGQKRIVKMDPEDI-TAKAVIIATGSTNRKLGIPGEEEYSGRGVSYCAVCDGAFFKDENVAVVGGGDSAISEGLYLA 162
Cdd:TIGR01292 81 VDKSDRPFKVYTGDGKEyTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 163 NLAKDVDVIHRRDQLRAERVLQTRAFKNPKMEFTWDSVPVEIIGDeNKVTGVKVHNKKTDEDKVIDASGVFIYIGNVPNS 242
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGD-NKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 243 EPFKELKITDDQGWIITNDQMETTVPGIYAVGDVRQKKLRQIVTAVGDGGIAGQNAFEYI 302
Cdd:TIGR01292 240 ELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
1-305 |
3.48e-92 |
|
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: 283.98 E-value: 3.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKE-YDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNTAEVENYPGFPSIMGPDLGEKMYKSATKQGVEFVYG 79
Cdd:TIGR03143 1 MEEiYDLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 80 DVQKIELDGQKRIVKMDPEDITAKAVIIATGSTNRKLGIPGEEEYSGRGVSYCAVCDGAFFKDENVAVVGGGDSAISEGL 159
Cdd:TIGR03143 81 EVLDVDFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 160 YLANLAKDVDVIHRRDQLRAERVLQTRAFKNPKMEFTWDSVPVEIIGDEnKVTGVKVHNKKTDEDKVIDAS------GVF 233
Cdd:TIGR03143 161 FLTRYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDD-GLRYAKFVNNVTGEITEYKAPkdagtfGVF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489725795 234 IYIGNVPNSEPFKELKITDDQGWIITNDQMETTVPGIYAVGDVRQKKLRQIVTAVGDGGIAGQNAFEYISEL 305
Cdd:TIGR03143 240 VFVGYAPSSELFKGVVELDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKEL 311
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
4-302 |
2.18e-76 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 241.99 E-value: 2.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMI-DRgvYGGQMNNTAEVENYPGFPSIMGPDLGEKMyKSATKQgvefvYgDVQ 82
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVaER--FGGQVLDTMGIENFISVPETEGPKLAAAL-EEHVKE-----Y-DVD 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 83 KIELdgqKRIVKMDPED------------ITAKAVIIATGSTNRKLGIPGEEEYSGRGVSYCAVCDGAFFKDENVAVVGG 150
Cdd:PRK15317 283 IMNL---QRASKLEPAAglievelangavLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGG 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 151 GDSAISEGLYLANLAKDVDVIHRRDQLRAERVLQTRAFKNPKMEFTWDSVPVEIIGDENKVTGVKVHNKKTDEDKVIDAS 230
Cdd:PRK15317 360 GNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELE 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489725795 231 GVFIYIGNVPNSEPFKELKITDDQGWIITNDQMETTVPGIYAVGDVRQKKLRQIVTAVGDGGIAGQNAFEYI 302
Cdd:PRK15317 440 GVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
2-307 |
3.76e-72 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 225.33 E-value: 3.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 2 KEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNTAEVENYPGFPS-IMGPDLGEKMYKSATKQGVEFVYGD 80
Cdd:PRK10262 5 KHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNdLTGPLLMERMHEHATKFETEIIFDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 81 VQKIELDGQKRIVKMDPEDITAKAVIIATGSTNRKLGIPGEEEYSGRGVSYCAVCDGAFFKDENVAVVGGGDSAISEGLY 160
Cdd:PRK10262 85 INKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 161 LANLAKDVDVIHRRDQLRAERVLQTRAF---KNPKMEFTWDSVPVEIIGDENKVTGVKVHN-KKTDEDKVIDASGVFIYI 236
Cdd:PRK10262 165 LSNIASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQMGVTGVRLRDtQNSDNIESLDVAGLFVAI 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489725795 237 GNVPNSEPFkELKITDDQGWI-----ITNDQMETTVPGIYAVGDVRQKKLRQIVTAVGDGGIAGQNAFEYISELTD 307
Cdd:PRK10262 245 GHSPNTAIF-EGQLELENGYIkvqsgIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLAD 319
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
4-291 |
2.94e-61 |
|
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: 196.77 E-value: 2.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVY--GGQMNNTAEVENYPGFPSIM--GPDLGEKMYKSATKQGVE-FVY 78
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcpYGGCVLSKALLGAAEAPEIAslWADLYKRKEEVVKKLNNGiEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 79 GDVQKIELD-GQKRIVKMDP-----EDITAKAVIIATGSTNRKLGIPGEEEYSGRGVSYCAVCDGAFFK--DENVAVVGG 150
Cdd:pfam07992 81 LGTEVVSIDpGAKKVVLEELvdgdgETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 151 GDSAISEGLYLANLAKDVDVIHRRDQL------RAERVLQtRAFKNPKMEFTWDSVPVEIIGDENKVTgvkvhnKKTDED 224
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALE-KALEKNGVEVRLGTSVKEIIGDGDGVE------VILKDG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489725795 225 KVIDASGVFIYIGNVPNSEPFKELKI-TDDQGWIITNDQMETTVPGIYAVGDVRQKKLRQIVTAVGDG 291
Cdd:pfam07992 234 TEIDADLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-299 |
9.56e-40 |
|
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: 144.46 E-value: 9.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGG------------------QMNNTAEVENY---PGFPSIMGP 59
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGtclnvgcipskallhaaeVAHEARHAAEFgisAGAPSVDWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 60 D-----------LGEKMYKSATKQGVEFVYGDVqkiELDGQKRIVKMDPEDITAKAVIIATGSTNRKLGIPGEEEysGRG 128
Cdd:COG1249 81 AlmarkdkvvdrLRGGVEELLKKNGVDVIRGRA---RFVDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDE--VRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 129 VSYcavcDGAFFKDE---NVAVVGGGdsAIseGL----YLANLAKDVDVIHRRDQ-LRAE-----RVLQtRAFKNPKMEF 195
Cdd:COG1249 156 LTS----DEALELEElpkSLVVIGGG--YI--GLefaqIFARLGSEVTLVERGDRlLPGEdpeisEALE-KALEKEGIDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 196 TWDSVPVEIIGDENkvtGVKVHNKKTDEDKVIDASGVFIYIGNVPNSEPF--KELKI-TDDQGWIITNDQMETTVPGIYA 272
Cdd:COG1249 227 LTGAKVTSVEKTGD---GVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLglEAAGVeLDERGGIKVDEYLRTSVPGIYA 303
|
330 340
....*....|....*....|....*...
gi 489725795 273 VGDVRQKklRQIV-TAVGDGGIAGQNAF 299
Cdd:COG1249 304 IGDVTGG--PQLAhVASAEGRVAAENIL 329
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-304 |
5.01e-35 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 131.84 E-value: 5.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNN-----------TAEV----ENYPGF---PSIMGPDLG 62
Cdd:PRK06292 1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNvgcipskaliaAAEAfheaKHAEEFgihADGPKIDFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 63 EKMYKSATKQG--VEFVYGDVQKIE----LDGQKRI-----VKMDPEDITAKAVIIATGStnRKLGIPGEEEYSGRG-VS 130
Cdd:PRK06292 81 KVMARVRRERDrfVGGVVEGLEKKPkidkIKGTARFvdpntVEVNGERIEAKNIVIATGS--RVPPIPGVWLILGDRlLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 131 YcavcDGAFFKD---ENVAVVGGGdsAIS-E-GLYLANLAKDVDVIHRRDQL----------RAERVLQTRafknpkMEF 195
Cdd:PRK06292 159 S----DDAFELDklpKSLAVIGGG--VIGlElGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE------FKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 196 tWDSVPVEIIGDENKVtgVKVHNKKTDEDKVIDASGVFIYIGNVPNSEP--FKELKI-TDDQGWIITNDQMETTVPGIYA 272
Cdd:PRK06292 227 -KLGAKVTSVEKSGDE--KVEELEKGGKTETIEADYVLVATGRRPNTDGlgLENTGIeLDERGRPVVDEHTQTSVPGIYA 303
|
330 340 350
....*....|....*....|....*....|...
gi 489725795 273 VGDVRQKK-LRQivTAVGDGGIAGQNAFEYISE 304
Cdd:PRK06292 304 AGDVNGKPpLLH--EAADEGRIAAENAAGDVAG 334
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
3-276 |
6.98e-28 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 112.16 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGG------------------QMNNTAEVENYPGFPSIMGPDLG-- 62
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGtclnrgcipskallhaaeRADEARHSEDFGIKAENVGIDFKkv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 63 --------EKMYKSAT----KQGVEFVYG-----DVQKIELDGQKrivkmDPEDITAKAVIIATGStnRKLGIPGEEeYS 125
Cdd:PRK06416 84 qewkngvvNRLTGGVEgllkKNKVDIIRGeaklvDPNTVRVMTED-----GEQTYTAKNIILATGS--RPRELPGIE-ID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 126 GRGVSYCavcDGAFFKDE---NVAVVGGGdsAIseGLYLA----NLAKDVDVIHRRDQLRAE------RVLQtRAFKNPK 192
Cdd:PRK06416 156 GRVIWTS---DEALNLDEvpkSLVVIGGG--YI--GVEFAsayaSLGAEVTIVEALPRILPGedkeisKLAE-RALKKRG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 193 MEFTWDSVPVEIIGDENkvtGVKVHNKKTDEDKVIDASGVFIYIGNVPNSEP--FKELKITDDQGWIITNDQMETTVPGI 270
Cdd:PRK06416 228 IKIKTGAKAKKVEQTDD---GVTVTLEDGGKEETLEADYVLVAVGRRPNTENlgLEELGVKTDRGFIEVDEQLRTNVPNI 304
|
....*.
gi 489725795 271 YAVGDV 276
Cdd:PRK06416 305 YAIGDI 310
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
8-307 |
1.11e-26 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 108.73 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDR-----GV--YGgqmnntaevenYPGF--PSimgpDLGEKMYKSATKQGVEFVY 78
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTIFEArdkagGLlrYG-----------IPEFrlPK----DIVDREVERLLKLGVEIRT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 79 GdvQKIEldgqkRIVKMDpeDITA--KAVIIATGSTN-RKLGIPGEEEysgRGVsYCAV----------CDGAFFKDENV 145
Cdd:PRK11749 210 N--TEVG-----RDITLD--ELRAgyDAVFIGTGAGLpRFLGIPGENL---GGV-YSAVdfltrvnqavADYDLPVGKRV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 146 AVVGGGD-------SAISEGlylanlAKDVDVIHRRDqlRAERVLQTRAFKNPKME---FTWDSVPVEIIGDENKVTGVK 215
Cdd:PRK11749 277 VVIGGGNtamdaarTAKRLG------AESVTIVYRRG--REEMPASEEEVEHAKEEgveFEWLAAPVEILGDEGRVTGVE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 216 VHN--------------KKTDEDKVIDASGVFIYIGNVPNS---EPFKELKITDDQGWIITNDQMETTVPGIYAVGD-VR 277
Cdd:PRK11749 349 FVRmelgepdasgrrrvPIEGSEFTLPADLVIKAIGQTPNPlilSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDiVT 428
|
330 340 350
....*....|....*....|....*....|
gi 489725795 278 QKKLrqIVTAVGDGGIAGQNAFEYISELTD 307
Cdd:PRK11749 429 GAAT--VVWAVGDGKDAAEAIHEYLEGAAS 456
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
3-279 |
2.52e-26 |
|
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: 107.73 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNN-----------TAEVENYPGFPSIMGPDLG------EKM 65
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNvgciptkallhSAEVYDEIKHAKDLGIEVEnvsvdwEKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 66 YKSATK------QGVEF--------VYGDVQKIELDGQKRIVKMDPED-ITAKAVIIATGSTNRKLgiPGEEEYSGRGV- 129
Cdd:TIGR01350 81 QKRKNKvvkklvGGVSGllkknkvtVIKGEAKFLDPGTVSVTGENGEEtLEAKNIIIATGSRPRSL--PGPFDFDGKVVi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 130 -SycavcDGAFF---KDENVAVVGGGDSAISEGLYLANLAKDVDVIHRRDQL------RAERVLQtRAFKNPKMEFTWDS 199
Cdd:TIGR01350 159 tS-----TGALNleeVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRIlpgedaEVSKVLQ-KALKKKGVKILTNT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 200 VPVEIIGDENKVTgvkVHNKKTDEDKvIDASGVFIYIGNVPNSEPF--KELKI-TDDQGWIITNDQMETTVPGIYAVGDV 276
Cdd:TIGR01350 233 KVTAVEKNDDQVT---YENKGGETET-LTGEKVLVAVGRKPNTEGLglEKLGVeLDERGRIVVDEYMRTNVPGIYAIGDV 308
|
...
gi 489725795 277 RQK 279
Cdd:TIGR01350 309 IGG 311
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
8-291 |
9.40e-26 |
|
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: 105.99 E-value: 9.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDR-----GV--YGgqmnntaevenYPGFpsimgpdlgeKMYKSA--------TKQ 72
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEAldkpgGLlrYG-----------IPEF----------RLPKDVldreieliEAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 73 GVEFVYGdvqkieldgqKRIVKmdpeDITAK-------AVIIATGST-NRKLGIPGEEE---YSG----RGVSYCAVCDG 137
Cdd:COG0493 185 GVEFRTN----------VEVGK----DITLDelleefdAVFLATGAGkPRDLGIPGEDLkgvHSAmdflTAVNLGEAPDT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 138 AFFKDENVAVVGGGD-------SAISEGlylanlAKDVDVIHRRDQ----LRAERVlqtrafKNPKME---FTWDSVPVE 203
Cdd:COG0493 251 ILAVGKRVVVIGGGNtamdcarTALRLG------AESVTIVYRRTReempASKEEV------EEALEEgveFLFLVAPVE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 204 IIGDEN-KVTGVKVHN---------------KKTDEDKVIDASGVFIYIGNVPNSEPFKE-LKI-TDDQGWIITNDQ-ME 264
Cdd:COG0493 319 IIGDENgRVTGLECVRmelgepdesgrrrpvPIEGSEFTLPADLVILAIGQTPDPSGLEEeLGLeLDKRGTIVVDEEtYQ 398
|
330 340
....*....|....*....|....*...
gi 489725795 265 TTVPGIYAVGD-VRQKKLrqIVTAVGDG 291
Cdd:COG0493 399 TSLPGVFAGGDaVRGPSL--VVWAIAEG 424
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-276 |
3.44e-23 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 98.69 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMT----AAMYGAranlKVAMID----------RG-------VYGGQMnntAE-VENY-PGFpsim 57
Cdd:PRK06116 2 TKDYDLIVIGGGSGGIAsanrAAMYGA----KVALIEakrlggtcvnVGcvpkklmWYGAQI---AEaFHDYaPGY---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 58 GPDLGEKMYKSAT---------------------KQGVEFVYG-----DVQKIELDGQKrivkmdpedITAKAVIIATGS 111
Cdd:PRK06116 71 GFDVTENKFDWAKlianrdayidrlhgsyrngleNNGVDLIEGfarfvDAHTVEVNGER---------YTADHILIATGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 112 TNRKLGIPGEEeysgrgvsYCAVCDGAFFKDE---NVAVVGGGDSAISeglyLAN----LAKDVDVIHRR-------DQL 177
Cdd:PRK06116 142 RPSIPDIPGAE--------YGITSDGFFALEElpkRVAVVGAGYIAVE----FAGvlngLGSETHLFVRGdaplrgfDPD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 178 RAERVLQTRAFKNPKMEFtwDSVPVEIIGDENKVTGVKVHNKKTDE-DKVIDAsgvfiyIGNVPNSEPFKELKI---TDD 253
Cdd:PRK06116 210 IRETLVEEMEKKGIRLHT--NAVPKAVEKNADGSLTLTLEDGETLTvDCLIWA------IGREPNTDGLGLENAgvkLNE 281
|
330 340
....*....|....*....|...
gi 489725795 254 QGWIITNDQMETTVPGIYAVGDV 276
Cdd:PRK06116 282 KGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
8-291 |
5.96e-22 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 95.23 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDR-----GV--YGgqmnntaevenYPGFpsimgpdlgeKMYKSA--------TKQ 72
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVFERadrigGLlrYG-----------IPDF----------KLEKEVidrrielmEAE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 73 GVEFVYGdvqkIELDgqkriVKMDPEDITAK--AVIIATGSTN-RKLGIPGEEeysGRGVsYCAV-------------CD 136
Cdd:PRK12810 207 GIEFRTN----VEVG-----KDITAEELLAEydAVFLGTGAYKpRDLGIPGRD---LDGV-HFAMdfliqntrrvlgdET 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 137 GAFF--KDENVAVVGGGD-------SAISEGlylanlAKDVdviHRRD---QLRAERVLQTRAFKNPKM----------- 193
Cdd:PRK12810 274 EPFIsaKGKHVVVIGGGDtgmdcvgTAIRQG------AKSV---TQRDimpMPPSRRNKNNPWPYWPMKlevsnaheegv 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 194 EFTWDSVPVEIIGDENKVTGVKVHN---------KKTDEDKVIDASGVFIYIGNVPNSEP-FKELKI-TDDQGWIITND- 261
Cdd:PRK12810 345 EREFNVQTKEFEGENGKVTGVKVVRtelgegdfePVEGSEFVLPADLVLLAMGFTGPEAGlLAQFGVeLDERGRVAAPDn 424
|
330 340 350
....*....|....*....|....*....|.
gi 489725795 262 QMETTVPGIYAVGD-VRQKKLrqIVTAVGDG 291
Cdd:PRK12810 425 AYQTSNPKVFAAGDmRRGQSL--VVWAIAEG 453
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
4-299 |
1.45e-21 |
|
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: 94.41 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGG-----------------QMNNTAEVENYPGFPSIMGPDLGEKM- 65
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGtcvnvgcvpskmllraaEVAHYARKPPFGGLAATVAVDFGELLe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 66 -------------YKSATKQ-GVEFVYG-----DVQKIELDGQKRIVkmdpediTAKAVIIATGSTNRKLGIPGEEEysg 126
Cdd:TIGR02053 81 gkrevveelrhekYEDVLSSyGVDYLRGrarfkDPKTVKVDLGREVR-------GAKRFLIATGARPAIPPIPGLKE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 127 rgVSYcaVCDGAFFKD----ENVAVVGGGDSAISEGLYLANLAKDVDVIHRRDQLRAER-----VLQTRAFKNPKMEFTw 197
Cdd:TIGR02053 151 --AGY--LTSEEALALdripESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREepeisAAVEEALAEEGIEVV- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 198 DSVPVEIIGDENKvtGVKVHNKKTDEDKVIDASGVFIYIGNVPNSEPFKELKI---TDDQGWIITNDQMETTVPGIYAVG 274
Cdd:TIGR02053 226 TSAQVKAVSVRGG--GKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAgvkLDERGGILVDETLRTSNPGIYAAG 303
|
330 340
....*....|....*....|....*
gi 489725795 275 DVrQKKLRQIVTAVGDGGIAGQNAF 299
Cdd:TIGR02053 304 DV-TGGLQLEYVAAKEGVVAAENAL 327
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
26-276 |
7.29e-21 |
|
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: 90.64 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 26 NLKVAMIDRGVY-GGQmnntaeveNYPGFPSIMG--PDLGEKMYKSA---TKQGVEFVYGD-VQKIELDGQKRIVKmDPE 98
Cdd:COG0446 5 DAEITVIEKGPHhSYQ--------PCGLPYYVGGgiKDPEDLLVRTPesfERKGIDVRTGTeVTAIDPEAKTVTLR-DGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 99 DITAKAVIIATGSTNRKLGIPGeeeYSGRGVSYCAVCDGAF--------FKDENVAVVGGGdsAIseGL----YLANLAK 166
Cdd:COG0446 76 TLSYDKLVLATGARPRPPPIPG---LDLPGVFTLRTLDDADalrealkeFKGKRAVVIGGG--PI--GLelaeALRKRGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 167 DVDVIHRRDQL----------RAERVLQTRafknpKMEFTWDSVPVEIIGDEnkvtGVKVHnkkTDEDKVIDASGVFIYI 236
Cdd:COG0446 149 KVTLVERAPRLlgvldpemaaLLEEELREH-----GVELRLGETVVAIDGDD----KVAVT---LTDGEEIPADLVVVAP 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489725795 237 GNVPNSEPFKELKI-TDDQGWIITNDQMETTVPGIYAVGDV 276
Cdd:COG0446 217 GVRPNTELAKDAGLaLGERGWIKVDETLQTSDPDVYAAGDC 257
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-279 |
6.69e-20 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 89.49 E-value: 6.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNT-----------------AEVENYPGF--PSIMGPDL 61
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTgcvptktliasaraahlARRAAEYGVsvGGPVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 62 GEKMyksATKQGV--EFVYGDVQKI-ELDG-----------QKRIVKMDPEDITAKAVIIATGSTNRKLGIPGEEEysgr 127
Cdd:PRK06370 83 KAVM---ARKRRIraRSRHGSEQWLrGLEGvdvfrgharfeSPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDE---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 128 gVSYCAvCDGAF---FKDENVAVVGGGdsAIseGLYLA----NLAKDVDVIHRRDQL------RAERVLQtRAFKNPKME 194
Cdd:PRK06370 156 -VGYLT-NETIFsldELPEHLVIIGGG--YI--GLEFAqmfrRFGSEVTVIERGPRLlpredeDVAAAVR-EILEREGID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 195 FTWDSvpvEIIGDENKVTGVKVHNKKTDEDKVIDASGVFIYIGNVPNSEpfkELKI------TDDQGWIITNDQMETTVP 268
Cdd:PRK06370 229 VRLNA---ECIRVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTD---DLGLeaagveTDARGYIKVDDQLRTTNP 302
|
330
....*....|.
gi 489725795 269 GIYAVGDVRQK 279
Cdd:PRK06370 303 GIYAAGDCNGR 313
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
8-304 |
3.28e-19 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 86.58 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMnntaEVENYPGF--PsIMGPDLGekmYKSATKQGVEF-----VYGD 80
Cdd:PRK12770 23 IIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGL----MLFGIPEFriP-IERVREG---VKELEEAGVVFhtrtkVCCG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 81 VQKIELDGQ---KRIVKMdpEDITAK--AVIIATGS-TNRKLGIPGEEE---YSG-------RGVSYCAVCDGAFFKDE- 143
Cdd:PRK12770 95 EPLHEEEGDefvERIVSL--EELVKKydAVLIATGTwKSRKLGIPGEDLpgvYSAleylfriRAAKLGYLPWEKVPPVEg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 144 -NVAVVGGGDSAISEGLYLANL-AKDVDVIHRR------------DQLRAERVlqtrafknpkmEFTWDSVPVEIIGdEN 209
Cdd:PRK12770 173 kKVVVVGAGLTAVDAALEAVLLgAEKVYLAYRRtineapagkyeiERLIARGV-----------EFLELVTPVRIIG-EG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 210 KVTGVKVHNKK---------------TDEDKVIDASGVFIYIGNVPNSePFK--ELKI-TDDQGWIITNDQMETTVPGIY 271
Cdd:PRK12770 241 RVEGVELAKMRlgepdesgrprpvpiPGSEFVLEADTVVFAIGEIPTP-PFAkeCLGIeLNRKGEIVVDEKHMTSREGVF 319
|
330 340 350
....*....|....*....|....*....|...
gi 489725795 272 AVGDVRQKKlRQIVTAVGDGGIAGQNAFEYISE 304
Cdd:PRK12770 320 AAGDVVTGP-SKIGKAIKSGLRAAQSIHEWLDL 351
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
80-274 |
4.49e-18 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 82.66 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 80 DVQKIELDGQKRIVKMDPEDITAKAVIIATG--STNRKLGIPgeeEYsgrGVSYCAVCDGAFFKDENVAVVGGGDSAISE 157
Cdd:pfam13738 97 EVTSVKKEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVP---EL---PKHYSYVKDFHPYAGQKVVVIGGYNSAVDA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 158 GLYLANLAKDVDVIHRRDQLRA--------------ERVLQTRAFKNPKMEFTwdsVPVEIIGDENkvTGVKVHnkkTDE 223
Cdd:pfam13738 171 ALELVRKGARVTVLYRGSEWEDrdsdpsyslspdtlNRLEELVKNGKIKAHFN---AEVKEITEVD--VSYKVH---TED 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489725795 224 DKVIDASGVFIY-IGNVPNSEPFKE-LKITDDQGWIITNDQ-METTVPGIYAVG 274
Cdd:pfam13738 243 GRKVTSNDDPILaTGYHPDLSFLKKgLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
5-301 |
1.71e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 82.11 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 5 DLVVIGAGPGGMTAA----MYGARAnlKVAMIDRgvyggqmnntaevENYPGFPSIM------GPDLGEKMYKSA----T 70
Cdd:COG1251 3 RIVIIGAGMAGVRAAeelrKLDPDG--EITVIGA-------------EPHPPYNRPPlskvlaGETDEEDLLLRPadfyE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 71 KQGVEFVYGD-VQKIelDGQKRIVKM-DPEDITAKAVIIATGSTNRKLGIPGEEeysGRGVSYC---AVCD---GAFFKD 142
Cdd:COG1251 68 ENGIDLRLGTrVTAI--DRAARTVTLaDGETLPYDKLVLATGSRPRVPPIPGAD---LPGVFTLrtlDDADalrAALAPG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 143 ENVAVVGGGdsAIseGLYLAN-LAK---DVDVIHRRDQL-------RAERVLQtRAFKNPKMEFTWDSVPVEIIGDEnKV 211
Cdd:COG1251 143 KRVVVIGGG--LI--GLEAAAaLRKrglEVTVVERAPRLlprqldeEAGALLQ-RLLEALGVEVRLGTGVTEIEGDD-RV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 212 TGVKvhnkkTDEDKVIDASGVFIYIGNVPNSEPFKELKITDDQGwIITNDQMETTVPGIYAVGDVrqkklrqivtAVGDG 291
Cdd:COG1251 217 TGVR-----LADGEELPADLVVVAIGVRPNTELARAAGLAVDRG-IVVDDYLRTSDPDIYAAGDC----------AEHPG 280
|
330
....*....|
gi 489725795 292 GIAGQNAFEY 301
Cdd:COG1251 281 PVYGRRVLEL 290
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
8-303 |
8.54e-17 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 80.45 E-value: 8.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDrgvyggQMNNTAEVENYpGFPSIMGP--DLGEKMYKSATKQGVefvygdvqKIE 85
Cdd:PRK12831 145 VIGSGPAGLTCAGDLAKMGYDVTIFE------ALHEPGGVLVY-GIPEFRLPkeTVVKKEIENIKKLGV--------KIE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 86 LD---GqkRIVKMDP--EDITAKAVIIATGS-TNRKLGIPGE--------EEYSGR---GVSYCAVCDGAFFKDENVAVV 148
Cdd:PRK12831 210 TNvvvG--KTVTIDEllEEEGFDAVFIGSGAgLPKFMGIPGEnlngvfsaNEFLTRvnlMKAYKPEYDTPIKVGKKVAVV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 149 GGGDSAISEGLYLANLAKDVDVIHRR--DQLRAeRVLQTRAFKNPKMEFTWDSVPVEIIGDEN-KVTGVKVHNKK----- 220
Cdd:PRK12831 288 GGGNVAMDAARTALRLGAEVHIVYRRseEELPA-RVEEVHHAKEEGVIFDLLTNPVEILGDENgWVKGMKCIKMElgepd 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 221 ----------TDEDKVIDASGVFIYIGNVPN---SEPFKELKItDDQGWIITNDQM-ETTVPGIYAVGDvrqkklrqIVT 286
Cdd:PRK12831 367 asgrrrpveiEGSEFVLEVDTVIMSLGTSPNpliSSTTKGLKI-NKRGCIVADEETgLTSKEGVFAGGD--------AVT 437
|
330 340
....*....|....*....|....
gi 489725795 287 -------AVGDGGIAGQNAFEYIS 303
Cdd:PRK12831 438 gaatvilAMGAGKKAAKAIDEYLS 461
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
1-276 |
3.36e-16 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 78.64 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRG--VYGGQMNNTA---------EVENYPGFPSIMGPD------LGE 63
Cdd:PRK07251 1 MLTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESkaMYGGTCINIGciptktllvAAEKNLSFEQVMATKntvtsrLRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 64 KMYKSATKQGVE-------FVYGDVQKIELdGQKRIvkmdpeDITAKAVIIATGSTNRKLGIPGEEE----YSGRGVSYC 132
Cdd:PRK07251 81 KNYAMLAGSGVDlydaeahFVSNKVIEVQA-GDEKI------ELTAETIVINTGAVSNVLPIPGLADskhvYDSTGIQSL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 133 AVcdgaffKDENVAVVGGGDSAIS-EGLYlANLAKDVDVIHRRDQL--RAERVLQTRA---FKNPKMEFTWDSVPVEIIG 206
Cdd:PRK07251 154 ET------LPERLGIIGGGNIGLEfAGLY-NKLGSKVTVLDAASTIlpREEPSVAALAkqyMEEDGITFLLNAHTTEVKN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489725795 207 DENKVTgVKVHNKKTDEDKVIDASgvfiyiGNVPNSEPFkELKITD----DQGWIITNDQMETTVPGIYAVGDV 276
Cdd:PRK07251 227 DGDQVL-VVTEDETYRFDALLYAT------GRKPNTEPL-GLENTDieltERGAIKVDDYCQTSVPGVFAVGDV 292
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-276 |
8.62e-16 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 77.12 E-value: 8.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRG-VYGG---------------------QMNNTAEVENYPGFPSIMG 58
Cdd:PRK05249 3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYrNVGGgcthtgtipskalreavlrliGFNQNPLYSSYRVKLRITF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 59 PDLGEKMYKSATKQ-----------GVEFVYG-----DVQKIELDGQKRIVkmdpEDITAKAVIIATGS-TNRKLGIPGE 121
Cdd:PRK05249 83 ADLLARADHVINKQvevrrgqyernRVDLIQGrarfvDPHTVEVECPDGEV----ETLTADKIVIATGSrPYRPPDVDFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 122 EEYsgrgvsycaVCDGaffkDE---------NVAVVGGGDSAISEGLYLANLAKDVDVIHRRDQ----LRAERV--LQTr 186
Cdd:PRK05249 159 HPR---------IYDS----DSilsldhlprSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRllsfLDDEISdaLSY- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 187 AFKNPKMEFTWDSVPVEIIGDENkvtGVKVH---NKKTDEDKVIDASGvfiYIGNVpnsepfKELKI------TDDQGWI 257
Cdd:PRK05249 225 HLRDSGVTIRHNEEVEKVEGGDD---GVIVHlksGKKIKADCLLYANG---RTGNT------DGLNLenagleADSRGQL 292
|
330
....*....|....*....
gi 489725795 258 ITNDQMETTVPGIYAVGDV 276
Cdd:PRK05249 293 KVNENYQTAVPHIYAVGDV 311
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
3-307 |
1.80e-14 |
|
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: 73.35 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMID------RGVYGGQMNNTAEVENYPG----FPSIMGPDL---------GE 63
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptpLGTRWGIGGTCVNVGCIPKklmhQAALLGQALkdsrnygwkVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 64 KMYKSATKQGVEFVYGDV-------------QKI-------ELDGQKRIVKMD----PEDITAKAVIIATGSTNRKLGIP 119
Cdd:TIGR01438 82 ETVKHDWKRLVEAVQNHIgslnwgyrvalreKKVkyenayaEFVDKHRIKATNkkgkEKIYSAERFLIATGERPRYPGIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 120 GEEEYsgrgvsyCAVCDGAF---FKDENVAVVGGGDSAISEGLYLANLAKDVDVIHRR------DQLRAERVLQTRAFKN 190
Cdd:TIGR01438 162 GAKEL-------CITSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSillrgfDQDCANKVGEHMEEHG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 191 PKMEFTWDSVPVEIIGDENKVTGVKVHNKKTDE-DKVIDAsgvfiyIGNVPNSEPFK----ELKITDDQGWIITNDQMET 265
Cdd:TIGR01438 235 VKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEyDTVLLA------IGRDACTRKLNlenvGVKINKKTGKIPADEEEQT 308
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489725795 266 TVPGIYAVGDVRQKKLRQIVTAVGDGGIAGQNAFEYISELTD 307
Cdd:TIGR01438 309 NVPYIYAVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICD 350
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-276 |
1.88e-14 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 73.42 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMID-------RGVYGGQMNNT---------AEVENYpgfpSIMGPDLGE- 63
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVgcipskallASSEEF----ENAGHHFADh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 64 ------------KMYKSATK------QGVEFV---------YGDVQKIELDGQKRIVKM---DPEDITAKAVIIATGSTN 113
Cdd:PRK06327 78 gihvdgvkidvaKMIARKDKvvkkmtGGIEGLfkknkitvlKGRGSFVGKTDAGYEIKVtgeDETVITAKHVIIATGSEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 114 RKL-GIPgeeeysgrgVSYCAVCD--GAFFKDE---NVAVVGGGdsAIseGLYLAN----LAKDVDVIHRRDQLRA---E 180
Cdd:PRK06327 158 RHLpGVP---------FDNKIILDntGALNFTEvpkKLAVIGAG--VI--GLELGSvwrrLGAEVTILEALPAFLAaadE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 181 RVLQTrAFKnpkmEFTWDSVPVEiigdenkvTGVKVHNKKTDEDKVI----DASG---------VFIYIGNVPNSEPFKE 247
Cdd:PRK06327 225 QVAKE-AAK----AFTKQGLDIH--------LGVKIGEIKTGGKGVSvaytDADGeaqtlevdkLIVSIGRVPNTDGLGL 291
|
330 340 350
....*....|....*....|....*....|..
gi 489725795 248 LK---ITDDQGWIITNDQMETTVPGIYAVGDV 276
Cdd:PRK06327 292 EAvglKLDERGFIPVDDHCRTNVPNVYAIGDV 323
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
8-297 |
7.61e-14 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 71.83 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDRG-VYGGQMNntaevenYpGFPSIMGP-DLGEKMYKSATKQGVEFVYG-----D 80
Cdd:PRK12771 142 VIGGGPAGLSAAYHLRRMGHAVTIFEAGpKLGGMMR-------Y-GIPAYRLPrEVLDAEIQRILDLGVEVRLGvrvgeD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 81 VQKIELDGQkrivkMDpeditakAVIIATG-STNRKLGIPGEEeySGRGVSycAVcdgAFFKD----------ENVAVVG 149
Cdd:PRK12771 214 ITLEQLEGE-----FD-------AVFVAIGaQLGKRLPIPGED--AAGVLD--AV---DFLRAvgegeppflgKRVVVIG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 150 GGDSAISeglyLANLAK-----DVDVIHRR------------DQLRAERVlqtrafknpkmEFTWDSVPVEIIGDENKVT 212
Cdd:PRK12771 275 GGNTAMD----AARTARrlgaeEVTIVYRRtredmpahdeeiEEALREGV-----------EINWLRTPVEIEGDENGAT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 213 GVKV----------HNK---KTDEDKVIDASGVFIYIGNVPNSEPFKELK-ITDDQGWIITND-QMETTVPGIYAVGDVr 277
Cdd:PRK12771 340 GLRVitvekmeldeDGRpspVTGEEETLEADLVVLAIGQDIDSAGLESVPgVEVGRGVVQVDPnFMMTGRPGVFAGGDM- 418
|
330 340
....*....|....*....|
gi 489725795 278 QKKLRQIVTAVGDGGIAGQN 297
Cdd:PRK12771 419 VPGPRTVTTAIGHGKKAARN 438
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
8-304 |
4.83e-13 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 69.39 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDrgvyggQMNNTAEVENYpGFPSIMGPdlgekmyKSATKQGVEFVYGDVQKIELD 87
Cdd:PRK12778 436 VIGSGPAGLSFAGDLAKRGYDVTVFE------ALHEIGGVLKY-GIPEFRLP-------KKIVDVEIENLKKLGVKFETD 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 88 ---GQKRIVKmDPEDITAKAVIIATGS-TNRKLGIPGEE--------EYSGRG---VSYCAVCDGAFFKDENVAVVGGGD 152
Cdd:PRK12778 502 vivGKTITIE-ELEEEGFKGIFIASGAgLPNFMNIPGENsngvmssnEYLTRVnlmDAASPDSDTPIKFGKKVAVVGGGN 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 153 SAISEGLYLANL-AKDVDVIHRRDQ----LRAERVLQTrafKNPKMEFTWDSVPVEIIGDEN-KVTGVKVHNKKTDEDkv 226
Cdd:PRK12778 581 TAMDSARTAKRLgAERVTIVYRRSEeempARLEEVKHA---KEEGIEFLTLHNPIEYLADEKgWVKQVVLQKMELGEP-- 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 227 iDASG------------------VFIYIGNVPN---SEPFKELKItDDQGWIITNDQMETTVPGIYAVGD-VRQKKlrQI 284
Cdd:PRK12778 656 -DASGrrrpvaipgstftvdvdlVIVSVGVSPNplvPSSIPGLEL-NRKGTIVVDEEMQSSIPGIYAGGDiVRGGA--TV 731
|
330 340
....*....|....*....|
gi 489725795 285 VTAVGDGGIAGQNAFEYISE 304
Cdd:PRK12778 732 ILAMGDGKRAAAAIDEYLSS 751
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
5-276 |
7.81e-12 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 65.15 E-value: 7.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 5 DLVVIGAGPGGMTAAMYGAR---ANLKVAMIDRGVY-----------GGQMNntaevenypgfPSIMGPDLgEKMYKsat 70
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYhlfqpllpevaAGTLS-----------PDDIAIPL-RELLR--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 71 KQGVEFVYGDVQKIELDgQKRIVKMDPEDITAKAVIIATGSTNRKLGIPGEEEYsgrGVSYCAVCDGAFFKDE------- 143
Cdd:COG1252 68 RAGVRFIQGEVTGIDPE-ARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEH---ALPLKTLEDALALRERllaafer 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 144 -------NVAVVGGGDSAIsEglYLANLAKDVDVIHRRDQLRAERVlqtrafknpkmEFTW-DSVPvEIIGD-------- 207
Cdd:COG1252 144 aerrrllTIVVVGGGPTGV-E--LAGELAELLRKLLRYPGIDPDKV-----------RITLvEAGP-RILPGlgeklsea 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 208 -----ENKvtGVKVHNKKT----DEDKVIDASGVFI---YI----GNVPNsEPFKELKI-TDDQGWIITNDQMETT-VPG 269
Cdd:COG1252 209 aekelEKR--GVEVHTGTRvtevDADGVTLEDGEEIpadTViwaaGVKAP-PLLADLGLpTDRRGRVLVDPTLQVPgHPN 285
|
....*..
gi 489725795 270 IYAVGDV 276
Cdd:COG1252 286 VFAIGDC 292
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
144-219 |
2.52e-10 |
|
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: 56.06 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 144 NVAVVGGGDSAISEGLYLANLAKDVDVIHRRDQLR------AERVLQTRAFKNpKMEFTWDSVPVEIIGDENKVtGVKVH 217
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGV-VVVLT 78
|
..
gi 489725795 218 NK 219
Cdd:pfam00070 79 DG 80
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
3-276 |
4.06e-10 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 60.27 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 3 EYDLVVIGAGPGGMTA----AMYGARA---NLKVAMID-------------RG-------VYGGQMNNtaEVENYPGFPS 55
Cdd:PLN02546 79 DFDLFTIGAGSGGVRAsrfaSNFGASAavcELPFATISsdtlggvggtcvlRGcvpkkllVYASKYSH--EFEESRGFGW 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 56 IMGPDLGEK-----MYKSATKQGVEFVYGDVQK------IEldGQKRIVkmDPEDI-------TAKAVIIATGSTNRKLG 117
Cdd:PLN02546 157 KYETEPKHDwntliANKNAELQRLTGIYKNILKnagvtlIE--GRGKIV--DPHTVdvdgklyTARNILIAVGGRPFIPD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 118 IPGEEeysgrgvsYCAVCDGAF---FKDENVAVVGGGDSAISEGLYLANLAKDVDVIhrrdqLRAERVL-----QTRAFK 189
Cdd:PLN02546 233 IPGIE--------HAIDSDAALdlpSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVF-----IRQKKVLrgfdeEVRDFV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 190 NPKM-----EFTWDSVPVEIIGDENKVTGVKVhNKKTdedkVIDASGVFIYIGNVPNSepfKELKI------TDDQGWII 258
Cdd:PLN02546 300 AEQMslrgiEFHTEESPQAIIKSADGSLSLKT-NKGT----VEGFSHVMFATGRKPNT---KNLGLeevgvkMDKNGAIE 371
|
330
....*....|....*...
gi 489725795 259 TNDQMETTVPGIYAVGDV 276
Cdd:PLN02546 372 VDEYSRTSVPSIWAVGDV 389
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
3-276 |
6.03e-10 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 59.58 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 3 EYDLVVIGAGPGGMtaaMYGAR-ANLKVAMIDRGVYGGQMNN-----------TAEVENYPGFPSIMGPDlgekmyksAT 70
Cdd:PRK07846 1 HYDLIIIGTGSGNS---ILDERfADKRIAIVEKGTFGGTCLNvgciptkmfvyAADVARTIREAARLGVD--------AE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 71 KQGVEF------VYGDVQKIELDG----------------------QKRIVKMDPEDITAKAVIIATGSTNRKLGIPGEE 122
Cdd:PRK07846 70 LDGVRWpdivsrVFGRIDPIAAGGeeyrgrdtpnidvyrgharfigPKTLRTGDGEEITADQVVIAAGSRPVIPPVIADS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 123 eysgrGVSYCAVCDGAFFKD--ENVAVVGGGDSAISEGLYLANLAKDVDVIHRRDQ-LRAERVLQTRAFkNPKMEFTWD- 198
Cdd:PRK07846 150 -----GVRYHTSDTIMRLPElpESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRlLRHLDDDISERF-TELASKRWDv 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 199 SVPVEIIGDENKVTGVKVhnkKTDEDKVIDASGVFIYIGNVPNSEPFKELKI---TDDQGWIITNDQMETTVPGIYAVGD 275
Cdd:PRK07846 224 RLGRNVVGVSQDGSGVTL---RLDDGSTVEADVLLVATGRVPNGDLLDAAAAgvdVDEDGRVVVDEYQRTSAEGVFALGD 300
|
.
gi 489725795 276 V 276
Cdd:PRK07846 301 V 301
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
4-283 |
8.84e-10 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 59.24 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNN----------------------------TAEVENYPGFP- 54
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNvgcvpkkimfnaasihdilensrhygfdTQFSFNLPLLVe 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 55 -----------------------------SIMGPDlgEKMYKSATKQGVEFVYGDVQKIELDGQKRIVKMDPEDITAKAV 105
Cdd:PTZ00058 129 rrdkyirrlndiyrqnlkkdnveyfegkgSLLSEN--QVLIKKVSQVDGEADESDDDEVTIVSAGVSQLDDGQVIEGKNI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 106 IIATGstnrklgipGEEEYSG-RGVSYCAVCDGaFFKDE---NVAVVGGGDSAISEGLYLANLAKDVDVIHRRDQ-LRA- 179
Cdd:PTZ00058 207 LIAVG---------NKPIFPDvKGKEFTISSDD-FFKIKeakRIGIAGSGYIAVELINVVNRLGAESYIFARGNRlLRKf 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 180 -ERVLQ--TRAFKNPKMEFTWDSVPVEIIGDENKVTGVKVhnkkTDEDKVIDASGVFIYIGNVPNSEPF--KELKITDDQ 254
Cdd:PTZ00058 277 dETIINelENDMKKNNINIITHANVEEIEKVKEKNLTIYL----SDGRKYEHFDYVIYCVGRSPNTEDLnlKALNIKTPK 352
|
330 340
....*....|....*....|....*....
gi 489725795 255 GWIITNDQMETTVPGIYAVGDVRQKKLRQ 283
Cdd:PTZ00058 353 GYIKVDDNQRTSVKHIYAVGDCCMVKKNQ 381
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
71-276 |
1.56e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 58.69 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 71 KQGVEfVYGDVQKIELDGQKRIVKMDPEDITA-KAVIIATGSTNRKLGIPGEEE---YSGRGVSYCAVCDGAFFKDENVA 146
Cdd:TIGR02374 66 KHGIT-LYTGETVIQIDTDQKQVITDAGRTLSyDKLILATGSYPFILPIPGADKkgvYVFRTIEDLDAIMAMAQRFKKAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 147 VVGGGDSAISEGLYLANLAKDVDVIHRRDQLRAERVLQT------RAFKNPKMEFTWDSVPVEIIGDeNKVTGVKVhnkk 220
Cdd:TIGR02374 145 VIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTagrllqRELEQKGLTFLLEKDTVEIVGA-TKADRIRF---- 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489725795 221 tDEDKVIDASGVFIYIGNVPNSEPFKELKITDDQGwIITNDQMETTVPGIYAVGDV 276
Cdd:TIGR02374 220 -KDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRG-IIVNDSMQTSDPDIYAVGEC 273
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
3-276 |
4.82e-09 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 57.13 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMID--------------------RG-------VYGGQM-------------- 41
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissesiggvggtcviRGcvpkkilVYGATFggefedaknygwei 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 42 -------------NNTAEVENYPGFPSIMGPDLGEKMYKSATKqgvefVYGD--VQKIELDGQKRivkmdpeDITAKAVI 106
Cdd:PLN02507 105 nekvdfnwkkllqKKTDEILRLNGIYKRLLANAGVKLYEGEGK-----IVGPneVEVTQLDGTKL-------RYTAKHIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 107 IATGSTNRKLGIPGEEeysgrgvsYCAVCDGAFFKDE---NVAVVGGGDSAISEGLYLANLAKDVDVIHRR--------D 175
Cdd:PLN02507 173 IATGSRAQRPNIPGKE--------LAITSDEALSLEElpkRAVVLGGGYIAVEFASIWRGMGATVDLFFRKelplrgfdD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 176 QLRA--ERVLQTRAFK-NPKMEFTwdsvPVEIIGDENKVTgvkvhnkkTDEDKVIDASGVFIYIGNVPNSepfKELKIT- 251
Cdd:PLN02507 245 EMRAvvARNLEGRGINlHPRTNLT----QLTKTEGGIKVI--------TDHGEEFVADVVLFATGRAPNT---KRLNLEa 309
|
330 340 350
....*....|....*....|....*....|
gi 489725795 252 -----DDQGWIITNDQMETTVPGIYAVGDV 276
Cdd:PLN02507 310 vgvelDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
143-275 |
5.24e-09 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 56.97 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 143 ENVAVVGGGDSAISEGLYLANLAKDVDVIHRRDqlraeRVLqTRAF------------KNPKMEFTWDSVPVEIIGdENK 210
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLED-----RIL-PDSFdkeitdvmeeelRENGVELHLNEFVKSLIG-EDK 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489725795 211 VTGVKVHNKKTDEDKVIDASGVfiyignVPNSEPFKELKI-TDDQGWIITNDQMETTVPGIYAVGD 275
Cdd:PRK09564 223 VEGVVTDKGEYEADVVIVATGV------KPNTEFLEDTGLkTLKNGAIIVDEYGETSIENIYAAGD 282
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
2-276 |
5.39e-09 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 56.90 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 2 KEYDLVVIGAGPGGM-----TAAMYGARanlkVAMID---------RGVYGGQMNNTAEVenyPGFPSIMGPDLGEKMYK 67
Cdd:TIGR01423 2 KAFDLVVIGAGSGGLeagwnAATLYKKR----VAVVDvqthhgppfYAALGGTCVNVGCV---PKKLMVTGAQYMDTLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 68 SA----------------------------TKQGVEFVYGDVQKIELD------GQKRIVKM----DP-----EDITAKA 104
Cdd:TIGR01423 75 SAgfgwefdrssvkanwkaliaaknkavldINKSYEGMFADTEGLTFFlgwgalEDKNVVLVresaDPksavkERLQAEH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 105 VIIATGSTNRKLGIPGEEeysgrgvsYCAVCDGAFFKDE---NVAVVGGGDSAIS-EGLYLANLAK--DVDVIHRRD--- 175
Cdd:TIGR01423 155 ILLATGSWPQMLGIPGIE--------HCISSNEAFYLDEpprRVLTVGGGFISVEfAGIFNAYKPRggKVTLCYRNNmil 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 176 -----QLRAERVLQTRAFKnpkmeftwdsvpVEIIGDEN--KVTGVKVHNKKT--DEDKVIDASGVFIYIGNVPNSEPFK 246
Cdd:TIGR01423 227 rgfdsTLRKELTKQLRANG------------INIMTNENpaKVTLNADGSKHVtfESGKTLDVDVVMMAIGRVPRTQTLQ 294
|
330 340 350
....*....|....*....|....*....|...
gi 489725795 247 ELKI---TDDQGWIITNDQMETTVPGIYAVGDV 276
Cdd:TIGR01423 295 LDKVgveLTKKGAIQVDEFSRTNVPNIYAIGDV 327
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
6-276 |
2.70e-08 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 54.48 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 6 LVVIGAGPGGMTAAMYGARANLKVAMIDR-GVYG-----------------GQMNNTAEVE----NYPGFPSiMGPDLG- 62
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERdGLGGaavltdcvpsktliataEVRTELRRAAelgiRFIDDGE-ARVDLPa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 63 -------------EKMYKSATKQGVEFVYGDVQ-KIELDGQKRIVKMDP----EDITAKAVIIATGSTNRKLgiPGeeey 124
Cdd:PRK07845 83 vnarvkalaaaqsADIRARLEREGVRVIAGRGRlIDPGLGPHRVKVTTAdggeETLDADVVLIATGASPRIL--PT---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 125 sgrgvsycAVCDGAFFKD-----------ENVAVVGGG-DSAISEGLYLAnLAKDVDVIHRRDQL------RAERVLQTr 186
Cdd:PRK07845 157 --------AEPDGERILTwrqlydldelpEHLIVVGSGvTGAEFASAYTE-LGVKVTLVSSRDRVlpgedaDAAEVLEE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 187 AFKNPKMEFTWDS--VPVEIIGDenkvtGVKVHnkkTDEDKVIDASGVFIYIGNVPNSEPFKELKI---TDDQGWIITND 261
Cdd:PRK07845 227 VFARRGMTVLKRSraESVERTGD-----GVVVT---LTDGRTVEGSHALMAVGSVPNTAGLGLEEAgveLTPSGHITVDR 298
|
330
....*....|....*
gi 489725795 262 QMETTVPGIYAVGDV 276
Cdd:PRK07845 299 VSRTSVPGIYAAGDC 313
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-82 |
2.73e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 54.86 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDR-GVYGGQMnNTAEVenyPGF-----PSIMG-PDLGEKMYKSA-TKQ 72
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGGRA-RTFER---PGFrfdvgPSVLTmPGVLERLFRELgLED 76
|
90
....*....|
gi 489725795 73 GVEFVYGDVQ 82
Cdd:COG1233 77 YLELVPLDPA 86
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
6-110 |
1.21e-07 |
|
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: 52.12 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 6 LVVIGAGPGGMTAAMYGARANLKVAMIDRgvyggqmnntaevenYPGFPSIMGPDLGEKMYKSATKQGVEFVYGD-VQKI 84
Cdd:COG0446 127 AVVIGGGPIGLELAEALRKRGLKVTLVER---------------APRLLGVLDPEMAALLEEELREHGVELRLGEtVVAI 191
|
90 100
....*....|....*....|....*.
gi 489725795 85 ELDGQKRIVKMDPEDITAKAVIIATG 110
Cdd:COG0446 192 DGDDKVAVTLTDGEEIPADLVVVAPG 217
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
8-304 |
2.11e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 52.08 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMID-RGVYGGQMNntaevenYpGFPSIMGPDlgekmykSATKQGVEFVYGDVQKIEL 86
Cdd:PRK13984 288 IVGSGPAGLSAAYFLATMGYEVTVYEsLSKPGGVMR-------Y-GIPSYRLPD-------EALDKDIAFIEALGVKIHL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 87 DgqKRIVKMDP-EDITAK--AVIIATGST-NRKLGIPGEEEYSG-------RGVSYCAVCDGAFFK-DENVAVVGGGDSA 154
Cdd:PRK13984 353 N--TRVGKDIPlEELREKhdAVFLSTGFTlGRSTRIPGTDHPDViqalpllREIRDYLRGEGPKPKiPRSLVVIGGGNVA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 155 ISEGLYLANLAK------DVDVI---HRRDQLRAErVLQTRAFKNPKMEFTWDSVPVEIIGDENKVTGVKV--------- 216
Cdd:PRK13984 431 MDIARSMARLQKmeygevNVKVTsleRTFEEMPAD-MEEIEEGLEEGVVIYPGWGPMEVVIENDKVKGVKFkkcvevfde 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 217 ---HNKKTDEDKVI--DASGVFIYIGNVPN----SEPFKElKITDDQGWIITNDQMETTVPGIYAVGDVRQKKlrQIVTA 287
Cdd:PRK13984 510 egrFNPKFDESDQIivEADMVVEAIGQAPDysylPEELKS-KLEFVRGRILTNEYGQTSIPWLFAGGDIVHGP--DIIHG 586
|
330
....*....|....*..
gi 489725795 288 VGDGGIAGQNAFEYISE 304
Cdd:PRK13984 587 VADGYWAAEGIDMYLRK 603
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
8-174 |
2.81e-07 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 51.65 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDRG-VYGGQMnntaevenYPGFP------SIMGPDLG--EKMyksatkqGVEFVY 78
Cdd:PRK12814 198 IIGAGPAGLTAAYYLLRKGHDVTIFDANeQAGGMM--------RYGIPrfrlpeSVIDADIAplRAM-------GAEFRF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 79 GDV--QKIELDGQKRivKMDpeditakAVIIATG-STNRKLGIPGEEEysgRGVsycaVCDGAFFKD----------ENV 145
Cdd:PRK12814 263 NTVfgRDITLEELQK--EFD-------AVLLAVGaQKASKMGIPGEEL---PGV----ISGIDFLRNvalgtalhpgKKV 326
|
170 180 190
....*....|....*....|....*....|
gi 489725795 146 AVVGGGDSAISEGLYLANL-AKDVDVIHRR 174
Cdd:PRK12814 327 VVIGGGNTAIDAARTALRLgAESVTILYRR 356
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
8-276 |
2.94e-07 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 51.87 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDR-GVYGGqmnntaeVENYpGFPSIMGP-DLGEKMYKSATKQGVEFVYGDVQkie 85
Cdd:PRK12775 435 ICGSGPAGLAAAADLVKYGVDVTVYEAlHVVGG-------VLQY-GIPSFRLPrDIIDREVQRLVDIGVKIETNKVI--- 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 86 ldGQKRIVKMDPEDITAKAVIIATGSTNRK-LGIPGEeeYSGRGVSYCAVC--------DGAFFKD------ENVAVVGG 150
Cdd:PRK12775 504 --GKTFTVPQLMNDKGFDAVFLGVGAGAPTfLGIPGE--FAGQVYSANEFLtrvnlmggDKFPFLDtpislgKSVVVIGA 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 151 GDSAIsEGLYLANL--AKDVDVIHRRDQLRA-ERVLQTRAFKNPKMEFTWDSVPVEIIGDEN-KVTGVKVHNKK------ 220
Cdd:PRK12775 580 GNTAM-DCLRVAKRlgAPTVRCVYRRSEAEApARIEEIRHAKEEGIDFFFLHSPVEIYVDAEgSVRGMKVEEMElgepde 658
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489725795 221 --------TDEDKVIDASGVFIYIGNVPN-----SEPFKELK----ITDDQGWIitNDQMETTVPGIYAVGDV 276
Cdd:PRK12775 659 kgrrkpmpTGEFKDLECDTVIYALGTKANpiitqSTPGLALNkwgnIAADDGKL--ESTQSTNLPGVFAGGDI 729
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-174 |
4.01e-07 |
|
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: 51.02 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRG--VyGG----------QMNNTAEVENYPGFPsiMGPDLGEKMYKS 68
Cdd:COG2072 4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKAddV-GGtwrdnrypglRLDTPSHLYSLPFFP--NWSDDPDFPTGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 69 ATKQGVEFV---YG---------DVQKIELDGQKR--IVKM-DPEDITAKAVIIATGSTNRKL--GIPGEEEYSGRGVSY 131
Cdd:COG2072 81 EILAYLEAYadkFGlrrpirfgtEVTSARWDEADGrwTVTTdDGETLTARFVVVATGPLSRPKipDIPGLEDFAGEQLHS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489725795 132 CAVCDGAFFKDENVAVVGGGDSAI---SEglyLANLAKDVDVIHRR 174
Cdd:COG2072 161 ADWRNPVDLAGKRVLVVGTGASAVqiaPE---LARVAAHVTVFQRT 203
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
143-284 |
6.04e-07 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 50.55 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 143 ENVAVVGGGDSA--ISEGLYLANLakDVDVIHRRDQLRAervLQTRAFKNPKM-EFTWDSVPVEIIGDENKVTGVKVHNK 219
Cdd:PRK13512 149 DKALVVGAGYISleVLENLYERGL--HPTLIHRSDKINK---LMDADMNQPILdELDKREIPYRLNEEIDAINGNEVTFK 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489725795 220 --KTDE-DKVIDAsgvfiyIGNVPNSEPFKELKIT-DDQGWIITNDQMETTVPGIYAVGDVRQKKLRQI 284
Cdd:PRK13512 224 sgKVEHyDMIIEG------VGTHPNSKFIESSNIKlDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
4-110 |
6.68e-07 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 50.27 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVY---------GGQMN--NTAE-----VENYPGFPSIMGP-------- 59
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKlgrkilisgGGRCNvtNLSEepdnfLSRYPGNPKFLKSalsrftpw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 60 ----------------DLGeKMY----KSAT----------KQGVEFVYG-DVQKIELDGQKRI-VKMDPEDITAKAVII 107
Cdd:pfam03486 81 dfiaffeslgvplkeeDHG-RLFpdsdKASDivdallnelkELGVKIRLRtRVLSVEKDDDGRFrVKTGGEELEADSLVL 159
|
...
gi 489725795 108 ATG 110
Cdd:pfam03486 160 ATG 162
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
11-123 |
1.05e-06 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 49.20 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 11 AGPGGMTAAMYGARANLKVAMIDRGVYGG-----------------QMNNTAEVENY-------------PGFPSIMGP- 59
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPGdkicgggllpraleelePLGLDEPLERPvrgarfyspggksVELPPGRGGg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489725795 60 ------DLGEKMYKSATKQGVEFVYG-DVQKIELDGQKRIVKM-DPEDITAKAVIIATG---STNRKLGIPGEEE 123
Cdd:COG0644 81 yvvdraRFDRWLAEQAEEAGAEVRTGtRVTDVLRDDGRVVVRTgDGEEIRADYVVDADGarsLLARKLGLKRRSD 155
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
3-39 |
1.82e-06 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 48.96 E-value: 1.82e-06
10 20 30
....*....|....*....|....*....|....*..
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGG 39
Cdd:PRK12843 16 EFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVG 52
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
4-307 |
2.39e-06 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 48.67 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMID------RGV---YGGQMNNTAEVE----NYPG-FPSIMGPDlgEKMYKSA 69
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstQGTkwgLGGTCVNVGCVPkklmHYAAnIGSIFHHD--SQMYGWK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 70 TKQ-----------------------------GVEFV-------------YGDVQKIELdgqkrivkmdpedITAKAVII 107
Cdd:PTZ00052 84 TSSsfnwgklvttvqnhirslnfsyrtglrssKVEYInglaklkdehtvsYGDNSQEET-------------ITAKYILI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 108 ATGS-TNRKLGIPGEEEYSgrgvsycAVCDGAFF--KDE-NVAVVGGGDSAISEGLYLANLAKDVDVIHRRDQLR----- 178
Cdd:PTZ00052 151 ATGGrPSIPEDVPGAKEYS-------ITSDDIFSlsKDPgKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRgfdrq 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 179 -AERVLQTraFKNPKMEFTWDSVPVEIIGDENKVTgVKVHNKKTDE-DKVIDASGVFIYIGNVpNSEPFKeLKITDDQGW 256
Cdd:PTZ00052 224 cSEKVVEY--MKEQGTLFLEGVVPINIEKMDDKIK-VLFSDGTTELfDTVLYATGRKPDIKGL-NLNAIG-VHVNKSNKI 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489725795 257 IITNDQmeTTVPGIYAVGDVRQKKLRQIVTAVGDGGIAGQNAFEYISELTD 307
Cdd:PTZ00052 299 IAPNDC--TNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFID 347
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
5-41 |
5.00e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 47.60 E-value: 5.00e-06
10 20 30
....*....|....*....|....*....|....*...
gi 489725795 5 DLVVIGAGPGGMTAAMYGARANLKVAMID-RGVYGGQM 41
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVErRGFLGGML 38
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-45 |
8.93e-06 |
|
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: 46.75 E-value: 8.93e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDR-GVYGGqmnNTA 45
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKvPPRGG---HTA 43
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-134 |
9.36e-06 |
|
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: 46.47 E-value: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDR------GVYGGQMN-NTAEV-------------------------- 47
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERappprpDGRGIALSpRSLELlrrlglwdrllargapirgirvrdgs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 48 ------------ENYPGFPSIMGPDLGEKMYKSATKQGVEFVYGD-VQKIELDGQKRIVKM-DPEDITAKAVIIATG--S 111
Cdd:COG0654 81 dgrvlarfdaaeTGLPAGLVVPRADLERALLEAARALGVELRFGTeVTGLEQDADGVTVTLaDGRTLRADLVVGADGarS 160
|
170 180
....*....|....*....|....
gi 489725795 112 TNRK-LGIPGEEEYSGRGVSYCAV 134
Cdd:COG0654 161 AVRRlLGIGFTGRDYPQRALWAGV 184
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
5-127 |
9.49e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 46.78 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 5 DLVVIGAGPGGMTAAMYGARANLKVAMI----DR-------------GVY---------GGQMNNTAE-------VENYP 51
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLIthntDTiaelscnpsiggiAKGhlvreidalGGLMGKAADktgiqfrMLNTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 52 GFPSIMGP----DlgEKMYKSATKQGVE------FVYGDVQKIELDGQK--RIVKMDPEDITAKAVIIATGSTNRKLGIP 119
Cdd:pfam01134 81 KGPAVRALraqvD--RDLYSKEMTETLEnhpnltLIQGEVTDLIPENGKvkGVVTEDGEEYKAKAVVLATGTFLNGKIHI 158
|
....*...
gi 489725795 120 GEEEYSGR 127
Cdd:pfam01134 159 GLKCYPAG 166
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
4-126 |
1.28e-05 |
|
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: 45.77 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMIDRG------VYGGQMNNTAEVENYPGFPSIMG------------------- 58
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKsfprykPCGGALSPRALEELDLPGELIVNlvrgarffspngdsveipi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 59 ----------PDLGEKMYKSATKQGVEFVYGDVQK---IELDGQKRIVKMDPEDITAKAVIIATGS---TNRKLGIPGEE 122
Cdd:TIGR02032 81 etelayvidrDAFDEQLAERAQEAGAELRLGTRVLdveIHDDRVVVIVRGSEGTVTAKIVIGADGSrsiVAKKLGLKKEP 160
|
....
gi 489725795 123 EYSG 126
Cdd:TIGR02032 161 REYG 164
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
6-275 |
2.40e-05 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 45.53 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 6 LVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNTAEV---------------ENYP---GFPSIMGPDLGEKMYK 67
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVpskimiraahiahlrRESPfdgGIAATVPTIDRSRLLA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 68 SATKQGVEFVYGDVQKIeLDGQKRIVKMDPE-------------------DITAKAVIIATGSTNRKLGIPGEeeysgRG 128
Cdd:PRK13748 181 QQQARVDELRHAKYEGI-LDGNPAITVLHGEarfkddqtlivrlndggerVVAFDRCLIATGASPAVPPIPGL-----KE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 129 VSYCAVCDgAFFKD---ENVAVVGGGDSAISEGLYLANLAKDVDVIHRR---------------DQLRAE--RVL---QT 185
Cdd:PRK13748 255 TPYWTSTE-ALVSDtipERLAVIGSSVVALELAQAFARLGSKVTILARStlffredpaigeavtAAFRAEgiEVLehtQA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 186 RAFKNPKMEFTWDSVPVEIIGDENKV-TGVKVHNKKTDedkvIDASGVfiyignvpnsepfkelkITDDQGWIITNDQME 264
Cdd:PRK13748 334 SQVAHVDGEFVLTTGHGELRADKLLVaTGRAPNTRSLA----LDAAGV-----------------TVNAQGAIVIDQGMR 392
|
330
....*....|.
gi 489725795 265 TTVPGIYAVGD 275
Cdd:PRK13748 393 TSVPHIYAAGD 403
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
260-305 |
4.14e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 45.04 E-value: 4.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489725795 260 NDQMETTVPGIYAVGDVRQKKLRQIVTAVGDGGIAGQNAFEYISEL 305
Cdd:PRK08275 362 NEKAETTVPGLYAAGDMASVPHNYMLGAFTYGWFAGENAAEYVAGR 407
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
2-35 |
8.01e-05 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 43.69 E-value: 8.01e-05
10 20 30
....*....|....*....|....*....|....
gi 489725795 2 KEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRG 35
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKG 34
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
5-39 |
8.71e-05 |
|
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: 43.82 E-value: 8.71e-05
10 20 30
....*....|....*....|....*....|....*
gi 489725795 5 DLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGG 39
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFG 35
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
3-39 |
1.16e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 43.64 E-value: 1.16e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRG-VYGG 39
Cdd:PRK12835 11 EVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSaHFGG 48
|
|
| solA |
PRK11259 |
N-methyl-L-tryptophan oxidase; |
1-34 |
1.44e-04 |
|
N-methyl-L-tryptophan oxidase;
Pssm-ID: 236887 [Multi-domain] Cd Length: 376 Bit Score: 42.90 E-value: 1.44e-04
10 20 30
....*....|....*....|....*....|....
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDR 34
Cdd:PRK11259 1 TMRYDVIVIGLGSMGSAAGYYLARRGLRVLGLDR 34
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
3-41 |
2.77e-04 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 41.69 E-value: 2.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARA-NLKVAMIDR------GVYGGQM 41
Cdd:pfam01946 17 ESDVVIVGAGSSGLTAAYYLAKNrGLKVAIIERsvspggGAWLGGQ 62
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-45 |
3.19e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 41.81 E-value: 3.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNTA 45
Cdd:PRK07494 5 KEHTDIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTTA 49
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
2-39 |
3.57e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 41.81 E-value: 3.57e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489725795 2 KEYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGG 39
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
|
|
| PLN02463 |
PLN02463 |
lycopene beta cyclase |
4-114 |
4.00e-04 |
|
lycopene beta cyclase
Pssm-ID: 178082 [Multi-domain] Cd Length: 447 Bit Score: 41.62 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 4 YDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNTA----EVEN----------YPG----------------F 53
Cdd:PLN02463 29 VDLVVVGGGPAGLAVAQQVSEAGLSVCCIDPSPLSIWPNNYGvwvdEFEAlglldcldttWPGavvyiddgkkkdldrpY 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489725795 54 PSIMGPDLGEKMYKSATKQGVEFVYGDVQKIE-LDGQKRIVKMDPEDITAKAVIIATGSTNR 114
Cdd:PLN02463 109 GRVNRKKLKSKMLERCIANGVQFHQAKVKKVVhEESKSLVVCDDGVKIQASLVLDATGFSRC 170
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
3-39 |
5.15e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 41.56 E-value: 5.15e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDR-GVYGG 39
Cdd:PRK07843 7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKaPHYGG 44
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
1-34 |
7.40e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 40.70 E-value: 7.40e-04
10 20 30
....*....|....*....|....*....|....
gi 489725795 1 MKEYDLVVIGAGPGGMTAAMYGARANLKVAMIDR 34
Cdd:PRK09126 1 MMHSDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
3-35 |
1.26e-03 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 40.16 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|...
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRG 35
Cdd:COG3075 2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAG 34
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
3-39 |
1.69e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 39.70 E-value: 1.69e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRG-VYGG 39
Cdd:PRK06134 12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGG 49
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
8-35 |
2.15e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 35.97 E-value: 2.15e-03
10 20
....*....|....*....|....*...
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDRG 35
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKR 28
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
63-116 |
2.44e-03 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 39.01 E-value: 2.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489725795 63 EKMYKSATKQGVEFVYG-DVQKIELDGqKRI--VKMDPEDITAKAVIIATGSTNRKL 116
Cdd:PRK00711 205 QRLAAMAEQLGVKFRFNtPVDGLLVEG-GRItgVQTGGGVITADAYVVALGSYSTAL 260
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
6-95 |
2.46e-03 |
|
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: 36.03 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 6 LVVIGAGPGGMTAAMYGARANLKVAMIDRGvyggqmnntaevenyPGFPSIMGPDLGEKMYKSATKQGVEFVYG-DVQKI 84
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERR---------------DRLLPGFDPEIAKILQEKLEKNGIEFLLNtTVEAI 66
|
90
....*....|.
gi 489725795 85 ELDGQKRIVKM 95
Cdd:pfam00070 67 EGNGDGVVVVL 77
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
8-110 |
2.55e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 39.46 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 8 VIGAGPGGMTAAMYGARANLKVAMIDR-GVYGGQMNNTAEVenypgFPSIMGPD--LGEKM-----------YKSATkqg 73
Cdd:COG1148 145 VIGGGIAGMTAALELAEQGYEVYLVEKePELGGRAAQLHKT-----FPGLDCPQciLEPLIaeveanpnitvYTGAE--- 216
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489725795 74 VEFVYGDVQ----KIELDGQKRIVkmdpedITAKAVIIATG 110
Cdd:COG1148 217 VEEVSGYVGnftvTIKKGPREEIE------IEVGAIVLATG 251
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
3-39 |
2.56e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 39.43 E-value: 2.56e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRG-VYGG 39
Cdd:PRK12839 8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKAsTCGG 45
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
141-296 |
2.80e-03 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 39.43 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 141 KDENVAVVGGGDSAISEGLYLANLAKDVDVIHRRDQlrAE---RVLQTRAFKNPKMEFTWDSVPVEIIGDE--NKVTGVK 215
Cdd:PRK12779 446 KGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRRTK--SEmpaRVEELHHALEEGINLAVLRAPREFIGDDhtHFVTHAL 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489725795 216 V--------------HNKKTDEDKVIDASGVFIYIGNVPN-----SEPfkELKiTDDQGWI-ITNDQMETTVPGIYAVGD 275
Cdd:PRK12779 524 LdvnelgepdksgrrSPKPTGEIERVPVDLVIMALGNTANpimkdAEP--GLK-TNKWGTIeVEKGSQRTSIKGVYSGGD 600
|
170 180
....*....|....*....|.
gi 489725795 276 VRQKKLRQIvTAVGDGGIAGQ 296
Cdd:PRK12779 601 AARGGSTAI-RAAGDGQAAAK 620
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
5-40 |
3.72e-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: 38.53 E-value: 3.72e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489725795 5 DLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQ 40
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| PRK10015 |
PRK10015 |
oxidoreductase; Provisional |
3-44 |
7.82e-03 |
|
oxidoreductase; Provisional
Pssm-ID: 182194 [Multi-domain] Cd Length: 429 Bit Score: 37.65 E-value: 7.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYGGQMNNT 44
Cdd:PRK10015 5 KFDAIVVGAGVAGSVAALVMARAGLDVLVIERGDSAGCKNMT 46
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
3-38 |
9.09e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 37.71 E-value: 9.09e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489725795 3 EYDLVVIGAGPGGMTAAMYGARANLKVAMIDRGVYG 38
Cdd:PRK07803 8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFG 43
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
65-111 |
9.71e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 37.19 E-value: 9.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489725795 65 MYKSATKQGVEFVYG-DVQKIELDGQK-RIVKMDPEDITAKAVIIATGS 111
Cdd:COG0665 157 LARAARAAGVRIREGtPVTGLEREGGRvTGVRTERGTVRADAVVLAAGA 205
|
|
| |
