|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
10-312 |
6.82e-157 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 440.33 E-value: 6.82e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTTEVENFPGFTEGIMGPELMQNMREQAEKFGAELRMELVT 89
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 90 KVELEGDVKKIWVDD-QEFQARTVILATGSAPRYLGVEGEQTLLGRGVSACATCDGFFFRDHHIAVIGGGDSAMEEADFL 168
Cdd:COG0492 81 SVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 169 TKFGSKVSIIHRRDEFRASAIMLERAKNNPKIEFVTNKTVSKVLGDTTVSGLELTDTVTGETSVLEATAMFVAIGHDPRS 248
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437404552 249 AMFRDV-VTTDAAGYVVVEhPSTKTNVPGVFAVGDLVDNHYQQAITAAGSGCRGAIDAEHYLAAL 312
Cdd:COG0492 241 ELLKGLgLELDEDGYIVVD-EDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
11-309 |
1.53e-153 |
|
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: 431.67 E-value: 1.53e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTTEVENFPGFTEGIMGPELMQNMREQAEKFGAELRMELVTK 90
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 91 VELEGDVKKIWVDD-QEFQARTVILATGSAPRYLGVEGEQTLLGRGVSACATCDGFFFRDHHIAVIGGGDSAMEEADFLT 169
Cdd:TIGR01292 81 VDKSDRPFKVYTGDgKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 170 KFGSKVSIIHRRDEFRASAIMLERAKNNPKIEFVTNKTVSKVLGDTTVSGLELTDTVTGETSVLEATAMFVAIGHDPRSA 249
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 250 MFRDVVTTDAAGYVVVEHpSTKTNVPGVFAVGDLVDNHYQQAITAAGSGCRGAIDAEHYL 309
Cdd:TIGR01292 241 LLKGLLELDENGYIVTDE-GMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
9-309 |
2.23e-93 |
|
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: 287.45 E-value: 2.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 9 IHDVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTTEVENFPGFTEgIMGPELMQNMREQAEKFGAELRMELV 88
Cdd:TIGR03143 4 IYDLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILN-TTGPELMQEMRQQAQDFGVKFLQAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 89 TKVELEGDVKKIWVDDQEFQARTVILATGSAPRYLGVEGEQTLLGRGVSACATCDGFFFRDHHIAVIGGGDSAMEEADFL 168
Cdd:TIGR03143 83 LDVDFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 169 TKFGSKVSIIHRRDEFRASAIMLERAKNNPKIEFVTNKTVSKVLGDTTVSGLELTDTVTGETSVLEATA------MFVAI 242
Cdd:TIGR03143 163 TRYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDDGLRYAKFVNNVTGEITEYKAPKdagtfgVFVFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437404552 243 GHDPRSAMFRDVVTTDAAGYVVVeHPSTKTNVPGVFAVGDLVDNHYQQAITAAGSGCRGAIDAEHYL 309
Cdd:TIGR03143 243 GYAPSSELFKGVVELDKRGYIPT-NEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYV 308
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
14-312 |
2.46e-88 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 266.93 E-value: 2.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 14 IIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTTEVENFPGFTEGIMGPELMQNMREQAEKFGAELRMELVTKVEL 93
Cdd:PRK10262 11 ILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINKVDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 94 EGDVKKIWVDDQEFQARTVILATGSAPRYLGVEGEQTLLGRGVSACATCDGFFFRDHHIAVIGGGDSAMEEADFLTKFGS 173
Cdd:PRK10262 91 QNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 174 KVSIIHRRDEFRASAIMLERAKN---NPKIEFVTNKTVSKVLGDTT-VSGLELTDTV-TGETSVLEATAMFVAIGHDPRS 248
Cdd:PRK10262 171 EVHLIHRRDGFRAEKILIKRLMDkveNGNIILHTNRTLEEVTGDQMgVTGVRLRDTQnSDNIESLDVAGLFVAIGHSPNT 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437404552 249 AMFRDVVTTDaAGYVVVEH----PSTKTNVPGVFAVGDLVDNHYQQAITAAGSGCRGAIDAEHYLAAL 312
Cdd:PRK10262 251 AIFEGQLELE-NGYIKVQSgihgNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGL 317
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
11-309 |
1.95e-60 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 200.77 E-value: 1.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKP-IVFEGIeyGGSLMTTTEVENFPGFTEgIMGPELMQNMREQAEKFGAELrMEL-- 87
Cdd:PRK15317 213 DVLVVGGGPAGAAAAIYAARKGIRTgIVAERF--GGQVLDTMGIENFISVPE-TEGPKLAAALEEHVKEYDVDI-MNLqr 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 88 VTKVELEGDVKKIWVDDQE-FQARTVILATGSAPRYLGVEGEQTLLGRGVSACATCDGFFFRDHHIAVIGGGDSAMEEAD 166
Cdd:PRK15317 289 ASKLEPAAGLIEVELANGAvLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAI 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 167 FLTKFGSKVSIIHRRDEFRASAIMLERAKNNPKIEFVTNKTVSKVLGDTT-VSGLELTDTVTGETSVLEATAMFVAIGHD 245
Cdd:PRK15317 369 DLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDkVTGLTYKDRTTGEEHHLELEGVFVQIGLV 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437404552 246 PRSAMFRDVVTTDAAGYVVVEHpSTKTNVPGVFAVGDLVDNHYQQAITAAGSGCRGAIDAEHYL 309
Cdd:PRK15317 449 PNTEWLKGTVELNRRGEIIVDA-RGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
10-298 |
9.55e-57 |
|
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: 185.21 E-value: 9.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFE---GIEYGGSLMTTTeVENFPGFTEGI-MGPELMQNMREQAEKFGAELRM 85
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEdegTCPYGGCVLSKA-LLGAAEAPEIAsLWADLYKRKEEVVKKLNNGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 86 EL---VTKVELEG----DVKKIWVDDQEFQARTVILATGSAPRYLGVEGEQTLLGRGVSACATCDGFFF--RDHHIAVIG 156
Cdd:pfam07992 80 LLgteVVSIDPGAkkvvLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLklLPKRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 157 GGDSAMEEADFLTKFGSKVSIIHRRDEF------RASAIMLERAKNNpKIEFVTNKTVSKVLGDTTVSgleltDTVTGET 230
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKN-GVEVRLGTSVKEIIGDGDGV-----EVILKDG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437404552 231 SVLEATAMFVAIGHDPRSAMFRDV-VTTDAAGYVVVEHpSTKTNVPGVFAVGDLVDNHYQQAITAAGSG 298
Cdd:pfam07992 234 TEIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDE-YLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
11-295 |
4.96e-29 |
|
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: 115.57 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGG-----------SLMTTTEV----ENFPGFteGIMG-------PEL 68
Cdd:COG1249 5 DLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGtclnvgcipskALLHAAEVaheaRHAAEF--GISAgapsvdwAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 69 MQNMREQAEKFGAELRMEL----VTKVELEG---DVKKIWV-DDQEFQARTVILATGSAPRYLGVEGeqtLLGRGVSaca 140
Cdd:COG1249 83 MARKDKVVDRLRGGVEELLkkngVDVIRGRArfvDPHTVEVtGGETLTADHIVIATGSRPRVPPIPG---LDEVRVL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 141 TCDGFFFRDH---HIAVIGGGDSAMEEADFLTKFGSKVSIIHRRDEF------RASAIMLERAKNNpKIEFVTNKTVSKV 211
Cdd:COG1249 157 TSDEALELEElpkSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpgedpEISEALEKALEKE-GIDILTGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 212 lgDTTVSGLELTDTVTGETSVLEATAMFVAIGhdpRSAMFRDV------VTTDAAGYVVV-EHpsTKTNVPGVFAVGDLV 284
Cdd:COG1249 236 --EKTGDGVTVTLEDGGGEEAVEADKVLVATG---RRPNTDGLgleaagVELDERGGIKVdEY--LRTSVPGIYAIGDVT 308
|
330
....*....|....*..
gi 1437404552 285 DNH------YQQAITAA 295
Cdd:COG1249 309 GGPqlahvaSAEGRVAA 325
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
11-282 |
1.75e-28 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 114.12 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGG-----------SLMTTTEV----ENFPGFteGIM-------GPEL 68
Cdd:PRK06292 5 DVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGtclnvgcipskALIAAAEAfheaKHAEEF--GIHadgpkidFKKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 69 MQNMREQAEKFGAELRMEL-----VTKVELEG---DVKKIWVDDQEFQARTVILATGSapRYLGVEGEQTLLGRGVsacA 140
Cdd:PRK06292 83 MARVRRERDRFVGGVVEGLekkpkIDKIKGTArfvDPNTVEVNGERIEAKNIVIATGS--RVPPIPGVWLILGDRL---L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 141 TCDGFFFRDH---HIAVIGGGDSAMEEADFLTKFGSKVSIIHRRD--------EFRASAI-MLERaknnpKIEFVTNKTV 208
Cdd:PRK06292 158 TSDDAFELDKlpkSLAVIGGGVIGLELGQALSRLGVKVTVFERGDrilpledpEVSKQAQkILSK-----EFKIKLGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 209 SKVlgDTTVSGLELTDTVTGETSVLEATAMFVAIGhdpRSAMFRDV------VTTDAAGYVVVeHPSTKTNVPGVFAVGD 282
Cdd:PRK06292 233 TSV--EKSGDEKVEELEKGGKTETIEADYVLVATG---RRPNTDGLglentgIELDERGRPVV-DEHTQTSVPGIYAAGD 306
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
12-305 |
5.83e-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: 106.76 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTtevenfpgfteGI----MGPELMQNMREQAEKFGAELRmel 87
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLRY-----------GIpefrLPKDVLDREIELIEALGVEFR--- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 88 vTKVELEGDVKkiwVDD--QEFQArtVILATGS-APRYLGVEGEQ-----------TLLGRGVSAcatcDGFFFRDHHIA 153
Cdd:COG0493 190 -TNVEVGKDIT---LDEllEEFDA--VFLATGAgKPRDLGIPGEDlkgvhsamdflTAVNLGEAP----DTILAVGKRVV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 154 VIGGGDSAMEEADFLTKFGSK-VSIIHRRDEFRASAIMLER--AKNNpKIEFVTNKTVSKVLGDTT--VSGLELTDT--- 225
Cdd:COG0493 260 VIGGGNTAMDCARTALRLGAEsVTIVYRRTREEMPASKEEVeeALEE-GVEFLFLVAPVEIIGDENgrVTGLECVRMelg 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 226 ------------VTGETSVLEATAMFVAIGHDPRSAMFRDV--VTTDAAGYVVVEHPSTKTNVPGVFAVGDLVdnHYQQ- 290
Cdd:COG0493 339 epdesgrrrpvpIEGSEFTLPADLVILAIGQTPDPSGLEEElgLELDKRGTIVVDEETYQTSLPGVFAGGDAV--RGPSl 416
|
330
....*....|....*..
gi 1437404552 291 AITAAGSGCRGA--IDA 305
Cdd:COG0493 417 VVWAIAEGRKAAraIDR 433
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
12-284 |
1.41e-24 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 102.95 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTtevenfpgfteGImgPE------LMQNMREQAEKFGAELRm 85
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLLRY-----------GI--PEfrlpkdIVDREVERLLKLGVEIR- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 86 elvTKVELEGDVKkiwVDD--QEFQArtVILATG-SAPRYLGVEGEQtlLGRGVSAC--------ATCDGFFFRDHHIAV 154
Cdd:PRK11749 209 ---TNTEVGRDIT---LDElrAGYDA--VFIGTGaGLPRFLGIPGEN--LGGVYSAVdfltrvnqAVADYDLPVGKRVVV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 155 IGGGDSAMEEADFLTKFGSK-VSIIHRRD--EFRASAIMLERAKNNpKIEFVTNKTVSKVLGD-TTVSGLELTDT----- 225
Cdd:PRK11749 279 IGGGNTAMDAARTAKRLGAEsVTIVYRRGreEMPASEEEVEHAKEE-GVEFEWLAAPVEILGDeGRVTGVEFVRMelgep 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 226 ---------VTGETSVLEATAMFVAIGHDPRSAMFRDV--VTTDAAGYVVVEHPSTKTNVPGVFAVGDLV 284
Cdd:PRK11749 358 dasgrrrvpIEGSEFTLPADLVIKAIGQTPNPLILSTTpgLELNRWGTIIADDETGRTSLPGVFAGGDIV 427
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
11-295 |
1.88e-24 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 102.53 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGG-----------SLMTTTEVenfpgftegimgpelMQNMREqAEKF 79
Cdd:PRK06416 6 DVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGtclnrgcipskALLHAAER---------------ADEARH-SEDF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 80 GaeLRMELVT----KVE-------------LEGDVKKIWVD---------------------DQEFQARTVILATGSAPR 121
Cdd:PRK06416 70 G--IKAENVGidfkKVQewkngvvnrltggVEGLLKKNKVDiirgeaklvdpntvrvmtedgEQTYTAKNIILATGSRPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 122 YL-GVEGEqtllGRGVsacATCDGFFFRDH---HIAVIGGGDSAMEEADFLTKFGSKVSIIHRRD-----EFRASAIMLE 192
Cdd:PRK06416 148 ELpGIEID----GRVI---WTSDEALNLDEvpkSLVVIGGGYIGVEFASAYASLGAEVTIVEALPrilpgEDKEISKLAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 193 RAKNNPKIEFVTNKTVSKVlgDTTVSGLELTDTVTGETSVLEATAMFVAIGHDPRSA----------MFRDVVTTDAAGy 262
Cdd:PRK06416 221 RALKKRGIKIKTGAKAKKV--EQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTEnlgleelgvkTDRGFIEVDEQL- 297
|
330 340 350
....*....|....*....|....*....|....*....
gi 1437404552 263 vvvehpstKTNVPGVFAVGDLVDN----H--YQQAITAA 295
Cdd:PRK06416 298 --------RTNVPNIYAIGDIVGGpmlaHkaSAEGIIAA 328
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
12-284 |
1.10e-22 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 97.54 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTtevenfpgfteGI----MGPELMQNMREQAEKFGaelrMEL 87
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGLLRY-----------GIpdfkLEKEVIDRRIELMEAEG----IEF 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 88 VTKVELEGDVKkiwVDD--QEFQArtVILATGS-APRYLGVEGE----------------QTLLGRGVSACATCDGfffr 148
Cdd:PRK12810 211 RTNVEVGKDIT---AEEllAEYDA--VFLGTGAyKPRDLGIPGRdldgvhfamdfliqntRRVLGDETEPFISAKG---- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 149 dHHIAVIGGGDSAMeeaDFL-TKFGSKVSIIHRRDEFRASAimLERAKNNPKIEFVTNKTVS----------------KV 211
Cdd:PRK12810 282 -KHVVVIGGGDTGM---DCVgTAIRQGAKSVTQRDIMPMPP--SRRNKNNPWPYWPMKLEVSnaheegverefnvqtkEF 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 212 LG-DTTVSGLELTDT---------VTGETSVLEATAMFVAIGHD-PRSAMFRDV-VTTDAAGYVVVEHPSTKTNVPGVFA 279
Cdd:PRK12810 356 EGeNGKVTGVKVVRTelgegdfepVEGSEFVLPADLVLLAMGFTgPEAGLLAQFgVELDERGRVAAPDNAYQTSNPKVFA 435
|
....*
gi 1437404552 280 VGDLV 284
Cdd:PRK12810 436 AGDMR 440
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
12-311 |
3.01e-19 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 87.77 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGI-EYGGSLmttteVENFPGF---TEGIMGPELmqnmrEQAEKFGaelrmel 87
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIFEALhEPGGVL-----VYGIPEFrlpKETVVKKEI-----ENIKKLG------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 88 vtkVELEGDV---KKIWVDD--QEFQARTVILATGSA-PRYLGVEGEQtlLGRGVSAcatcDGFFFR---------DHH- 151
Cdd:PRK12831 206 ---VKIETNVvvgKTVTIDEllEEEGFDAVFIGSGAGlPKFMGIPGEN--LNGVFSA----NEFLTRvnlmkaykpEYDt 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 152 -------IAVIGGGDSAMEEADFLTKFGSKVSIIHRR--DEFRASAIMLERAKN---------NPkIEFVT--NKTVSKV 211
Cdd:PRK12831 277 pikvgkkVAVVGGGNVAMDAARTALRLGAEVHIVYRRseEELPARVEEVHHAKEegvifdlltNP-VEILGdeNGWVKGM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 212 ------LGDTTVSGLELTDTVTGETSVLEATAMFVAIGHDPRSAMFRDV--VTTDAAGYVVVEHPSTKTNVPGVFAVGDL 283
Cdd:PRK12831 356 kcikmeLGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTkgLKINKRGCIVADEETGLTSKEGVFAGGDA 435
|
330 340
....*....|....*....|....*...
gi 1437404552 284 VDNHyQQAITAAGSGCRGAIDAEHYLAA 311
Cdd:PRK12831 436 VTGA-ATVILAMGAGKKAAKAIDEYLSK 462
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
151-225 |
6.60e-17 |
|
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: 74.16 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 151 HIAVIGGGDSAMEEADFLTKFGSKVSIIHRRDEFR------ASAIMLERAKNNpKIEFVTNKTVSKVLGDTTVSGLELTD 224
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
.
gi 1437404552 225 T 225
Cdd:pfam00070 80 G 80
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
11-295 |
6.90e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 80.19 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALyAARAElkpivfegiEYGGSLMTTTEvENFPGF-----TEGIMGPELMQNMREQAEKFGAELRM 85
Cdd:COG1251 3 RIVIIGAGMAGVRAAE-ELRKL---------DPDGEITVIGA-EPHPPYnrpplSKVLAGETDEEDLLLRPADFYEENGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 86 ELV--TKVE-LEGDVKKIWVDD-QEFQARTVILATGSAPRYLGVEGeqtLLGRGVsacatcdgFFFRD------------ 149
Cdd:COG1251 72 DLRlgTRVTaIDRAARTVTLADgETLPYDKLVLATGSRPRVPPIPG---ADLPGV--------FTLRTlddadalraala 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 150 --HHIAVIGGGDSAMEEADFLTKFGSKVSIIHRRDEF-------RASAIMLERAKNNpKIEFVTNKTVSKVLGDTTVSGL 220
Cdd:COG1251 141 pgKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQRLLEAL-GVEVRLGTGVTEIEGDDRVTGV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 221 ELTDtvtGETsvLEATAMFVAIGHDPRSAMFRDV-VTTDaAGYVVVEHpsTKTNVPGVFAVGD---------------LV 284
Cdd:COG1251 220 RLAD---GEE--LPADLVVVAIGVRPNTELARAAgLAVD-RGIVVDDY--LRTSDPDIYAAGDcaehpgpvygrrvleLV 291
|
330
....*....|.
gi 1437404552 285 DNHYQQAITAA 295
Cdd:COG1251 292 APAYEQARVAA 302
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
73-282 |
1.41e-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: 78.70 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 73 REQAEKFGAELRME-LVTKVELEGdvKKIWVDD-QEFQARTVILATGSAPRYLGVEGeqtLLGRGVSACATCDG------ 144
Cdd:COG0446 43 PESFERKGIDVRTGtEVTAIDPEA--KTVTLRDgETLSYDKLVLATGARPRPPPIPG---LDLPGVFTLRTLDDadalre 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 145 --FFFRDHHIAVIGGGDSAMEEADFLTKFGSKVSIIHRRD--------EFraSAIMLERAKNNpKIEFVTNKTVSKVLGD 214
Cdd:COG0446 118 alKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPrllgvldpEM--AALLEEELREH-GVELRLGETVVAIDGD 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437404552 215 TTVsGLELTDtvtGETsvLEATAMFVAIGHDPRSAMFRDV-VTTDAAGYVVVeHPSTKTNVPGVFAVGD 282
Cdd:COG0446 195 DKV-AVTLTD---GEE--IPADLVVVAPGVRPNTELAKDAgLALGERGWIKV-DETLQTSDPDVYAAGD 256
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
57-281 |
2.35e-14 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 71.87 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 57 PGFT---EGIMGPELMQNMREQAEKFGAELRM-ELVTKVELEGDVKKIWVDDQEFQARTVILATG--SAPRYLGVEgEQT 130
Cdd:pfam13738 63 PAFTfnrEHPSGNEYAEYLRRVADHFELPINLfEEVTSVKKEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVP-ELP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 131 LLGRGVSACATcdgffFRDHHIAVIGGGDSAMEEADFLTKFGSKVSIIHRRDEFRASAIM------------LERAKNNP 198
Cdd:pfam13738 142 KHYSYVKDFHP-----YAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDpsyslspdtlnrLEELVKNG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 199 KIEFVTNKTVSKVlgdtTVSGLELTDTVTGETSVLEATAMFVAIGHDPrSAMF--RDVVTTDAAGYVVVeHPST-KTNVP 275
Cdd:pfam13738 217 KIKAHFNAEVKEI----TEVDVSYKVHTEDGRKVTSNDDPILATGYHP-DLSFlkKGLFELDEDGRPVL-TEETeSTNVP 290
|
....*.
gi 1437404552 276 GVFAVG 281
Cdd:pfam13738 291 GLFLAG 296
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
12-305 |
1.98e-13 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 70.67 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFE-GIEYGGSLMTttevenfpgfteGIMGpelmqnMREQAEKFGAELRMELVTK 90
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEaGPKLGGMMRY------------GIPA------YRLPREVLDAEIQRILDLG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 91 VELEGDVkKIWVD------DQEFQArtVILATG-SAPRYLGVEGEQTllGRGVSACAtcdgfFFRD----------HHIA 153
Cdd:PRK12771 202 VEVRLGV-RVGEDitleqlEGEFDA--VFVAIGaQLGKRLPIPGEDA--AGVLDAVD-----FLRAvgegeppflgKRVV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 154 VIGGGDSAMEEADFLTKFG-SKVSIIHRR--DEFRASAIMLERAKNNpKIEFVTNKTVSKVLGD---------TTVSGLE 221
Cdd:PRK12771 272 VIGGGNTAMDAARTARRLGaEEVTIVYRRtrEDMPAHDEEIEEALRE-GVEINWLRTPVEIEGDengatglrvITVEKME 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 222 LTDT-----VTGETSVLEATAMFVAIGHDPRSAMFRDVV-TTDAAGYVVVEHPSTKTNVPGVFAVGDLV-DNHyqQAITA 294
Cdd:PRK12771 351 LDEDgrpspVTGEEETLEADLVVLAIGQDIDSAGLESVPgVEVGRGVVQVDPNFMMTGRPGVFAGGDMVpGPR--TVTTA 428
|
330
....*....|...
gi 1437404552 295 AGSGCRGA--IDA 305
Cdd:PRK12771 429 IGHGKKAArnIDA 441
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
96-289 |
2.02e-13 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 70.19 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 96 DVKKIWVDDQEFQARTVILATGSAPRYLGVEGEQTllgrgvsaCATCDGFFFRDH---HIAVIGGGDSAMEEADFLTKFG 172
Cdd:PRK06116 119 DAHTVEVNGERYTADHILIATGGRPSIPDIPGAEY--------GITSDGFFALEElpkRVAVVGAGYIAVEFAGVLNGLG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 173 SKVSIIHRRDEFRAS-------AIMLERAKNNPKIefVTNKTVSKV--LGDTTVSgLELTDtvtGETsvLEATAMFVAIG 243
Cdd:PRK06116 191 SETHLFVRGDAPLRGfdpdireTLVEEMEKKGIRL--HTNAVPKAVekNADGSLT-LTLED---GET--LTVDCLIWAIG 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1437404552 244 HDPRSAMF---RDVVTTDAAGYVVVEHPSTkTNVPGVFAVGDlVDNHYQ 289
Cdd:PRK06116 263 REPNTDGLgleNAGVKLNEKGYIIVDEYQN-TNVPGIYAVGD-VTGRVE 309
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
12-309 |
3.24e-13 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 70.16 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGI-EYGGSLmttteVENFPGF--TEGIMGPELmqnmrEQAEKFGaelrmelv 88
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFEALhEIGGVL-----KYGIPEFrlPKKIVDVEI-----ENLKKLG-------- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 89 tkVELEGDV---KKIWVDDQEFQA-RTVILATGSA-PRYLGVEGEQT--------LLGRGVSACATCDGF---FFRDHHI 152
Cdd:PRK12778 496 --VKFETDVivgKTITIEELEEEGfKGIFIASGAGlPNFMNIPGENSngvmssneYLTRVNLMDAASPDSdtpIKFGKKV 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 153 AVIGGGDSAMEEADFLTKFGS-KVSIIHRR--DEFRASAIMLERAK---------NNPkIEFVTNKT--VSKV------L 212
Cdd:PRK12778 574 AVVGGGNTAMDSARTAKRLGAeRVTIVYRRseEEMPARLEEVKHAKeegiefltlHNP-IEYLADEKgwVKQVvlqkmeL 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 213 GDTTVSGLELTDTVTGETSVLEATAMFVAIGHDPRSAMFRDV--VTTDAAGYVVVEhPSTKTNVPGVFAVGDLVDNHyQQ 290
Cdd:PRK12778 653 GEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIpgLELNRKGTIVVD-EEMQSSIPGIYAGGDIVRGG-AT 730
|
330
....*....|....*....
gi 1437404552 291 AITAAGSGCRGAIDAEHYL 309
Cdd:PRK12778 731 VILAMGDGKRAAAAIDEYL 749
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
11-282 |
1.10e-11 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 65.22 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFE-------------------------------GIEYGGSLMTTTEVEnfpgf 59
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIErgllggtcvntgcvptktliasaraahlarrAAEYGVSVGGPVSVD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 60 tegimGPELMQNMREQAEKF--GAELRMElvtkvELEG-DV----------KKIWVDDQEFQARTVILATGSAPRYLGVE 126
Cdd:PRK06370 82 -----FKAVMARKRRIRARSrhGSEQWLR-----GLEGvDVfrgharfespNTVRVGGETLRAKRIFINTGARAAIPPIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 127 G-EQTllgrgvsACATCDGFF---FRDHHIAVIGGGDSAMEEADFLTKFGSKVSIIHR------RDEFRASAImLERAKN 196
Cdd:PRK06370 152 GlDEV-------GYLTNETIFsldELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERgprllpREDEDVAAA-VREILE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 197 NPKIEFVTNKTVSKVlgDTTVSGLELTDTVTGETSVLEATAMFVAIGhdpRSAMFRDV------VTTDAAGYVVV-EHps 269
Cdd:PRK06370 224 REGIDVRLNAECIRV--ERDGDGIAVGLDCNGGAPEITGSHILVAVG---RVPNTDDLgleaagVETDARGYIKVdDQ-- 296
|
330
....*....|...
gi 1437404552 270 TKTNVPGVFAVGD 282
Cdd:PRK06370 297 LRTTNPGIYAAGD 309
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
12-309 |
1.19e-11 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 64.63 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMttteVENFPGFTegIMGPELMQNMREQAEKfGAELRMElvTKV 91
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLM----LFGIPEFR--IPIERVREGVKELEEA-GVVFHTR--TKV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 92 -------ELEGDV---KKIWVDD--QEFQArtVILATGS-APRYLGVEGEQtllGRGVsacatCDG--FFFRDH------ 150
Cdd:PRK12770 92 ccgeplhEEEGDEfveRIVSLEElvKKYDA--VLIATGTwKSRKLGIPGED---LPGV-----YSAleYLFRIRaaklgy 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 151 ------------HIAVIGGGDSAMEEADFLTKFGS-KVSIIHRR--DEFRASAIMLERAKNNpKIEFVTNKTVSKVLGDT 215
Cdd:PRK12770 162 lpwekvppvegkKVVVVGAGLTAVDAALEAVLLGAeKVYLAYRRtiNEAPAGKYEIERLIAR-GVEFLELVTPVRIIGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 216 TVSGLELTDT---------------VTGETSVLEATAMFVAIGHDPRSAMFRDV--VTTDAAGYVVV--EHpstKTNVPG 276
Cdd:PRK12770 241 RVEGVELAKMrlgepdesgrprpvpIPGSEFVLEADTVVFAIGEIPTPPFAKEClgIELNRKGEIVVdeKH---MTSREG 317
|
330 340 350
....*....|....*....|....*....|....
gi 1437404552 277 VFAVGDLVdnHYQQAI-TAAGSGCRGAIDAEHYL 309
Cdd:PRK12770 318 VFAAGDVV--TGPSKIgKAIKSGLRAAQSIHEWL 349
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
10-117 |
1.34e-11 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 64.75 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFE-G------------------------IEYG---------GSLMTTTE--- 52
Cdd:COG2509 31 YDVVIVGAGPAGLFAALELAEAGLKPLVLErGkdveertcpvaefwrkgkcnpesnIQFGeggagtfsdGKLNTRSKdpq 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 53 ----------VENfpGFTEGI-------MG----PELMQNMREQAEKFGAELRME-LVTKVELEGD-VKKIWVDD-QEFQ 108
Cdd:COG2509 111 gliryvleifVKF--GAPEEIlyaakphIGtdklPKVVKNIREYIEELGGEIRFNtRVTDILIEDGrVKGVVTNDgEEIE 188
|
....*....
gi 1437404552 109 ARTVILATG 117
Cdd:COG2509 189 ADAVILAPG 197
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
12-311 |
5.61e-11 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 63.21 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTttevENFPGF--TEGIMGPELmqnmrEQAEKFGAELRMELV- 88
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMR----YGIPRFrlPESVIDADI-----APLRAMGAEFRFNTVf 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 89 -TKVELEGdVKKiwvddqEFQArtVILATGSA-PRYLGVEGEQ--------TLLGRGVSACATCDGfffrdHHIAVIGGG 158
Cdd:PRK12814 267 gRDITLEE-LQK------EFDA--VLLAVGAQkASKMGIPGEElpgvisgiDFLRNVALGTALHPG-----KKVVVIGGG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 159 DSAMEEADFLTKFG-SKVSIIHRRDEFRASAimlerakNNPKIEFVTNKTVSKVLGDTTVS------GLELTDT------ 225
Cdd:PRK12814 333 NTAIDAARTALRLGaESVTILYRRTREEMPA-------NRAEIEEALAEGVSLRELAAPVSiersegGLELTAIkmqqge 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 226 -----------VTGETSVLEATAMFVAIGH--DPRSAMfRDVVTTDAAGYVVVEHPSTKTNVPGVFAVGDLVDNHyQQAI 292
Cdd:PRK12814 406 pdesgrrrpvpVEGSEFTLQADTVISAIGQqvDPPIAE-AAGIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGA-DIAI 483
|
330
....*....|....*....
gi 1437404552 293 TAAGSGCRGAIDAEHYLAA 311
Cdd:PRK12814 484 NAVEQGKRAAHAIDLFLNG 502
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
12-298 |
1.92e-10 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 61.77 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGI-EYGGSLMTttevenfpGFTEGIMGPELMQNMREQAEKFGAE-LRMELVT 89
Cdd:PRK12779 309 IAVVGSGPSGLINAYLLAVEGFPVTVFEAFhDLGGVLRY--------GIPEFRLPNQLIDDVVEKIKLLGGRfVKNFVVG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 90 KVELEGDVKK--IWvddqefqarTVILATGSA-PRYLGVEGEQTL-------------LGRGVSACATCDGFFFRDHHIA 153
Cdd:PRK12779 381 KTATLEDLKAagFW---------KIFVGTGAGlPTFMNVPGEHLLgvmsanefltrvnLMRGLDDDYETPLPEVKGKEVF 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 154 VIGGGDSAMEEADFLTKFGSKVSIIHRR--DEFRASAIMLERA----------------KNNPKIEFVTNKTVSKV-LGD 214
Cdd:PRK12779 452 VIGGGNTAMDAARTAKRLGGNVTIVYRRtkSEMPARVEELHHAleeginlavlraprefIGDDHTHFVTHALLDVNeLGE 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 215 TTVSGlELTDTVTGETSVLEATAMFVAIGHDPRSAMfRDV---VTTDAAGYVVVEHPSTKTNVPGVFAVGDLVDNHyQQA 291
Cdd:PRK12779 532 PDKSG-RRSPKPTGEIERVPVDLVIMALGNTANPIM-KDAepgLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGG-STA 608
|
....*..
gi 1437404552 292 ITAAGSG 298
Cdd:PRK12779 609 IRAAGDG 615
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
107-298 |
3.15e-10 |
|
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: 60.64 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 107 FQARTVILATGSAPRYLGVEGEQTLlgrgvsaCATCDGFF---FRDHHIAVIGGGDSAMEEADFLTKFGSKVSIIHR--- 180
Cdd:TIGR01438 142 YSAERFLIATGERPRYPGIPGAKEL-------CITSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRsil 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 181 ------------RDEFRASAIMLERAKNNPKIEFVTNKTVSKvLGDTTVSGLELTDTVtgetsvleatamFVAIGHDP-- 246
Cdd:TIGR01438 215 lrgfdqdcankvGEHMEEHGVKFKRQFVPIKVEQIEAKVLVE-FTDSTNGIEEEYDTV------------LLAIGRDAct 281
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437404552 247 RSAMFRD--VVTTDAAGYVVVEHPStKTNVPGVFAVGDLVDNHYQQAITAAGSG 298
Cdd:TIGR01438 282 RKLNLENvgVKINKKTGKIPADEEE-QTNVPYIYAVGDILEDKPELTPVAIQAG 334
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
6-309 |
4.14e-10 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 60.73 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 6 AGTIHDVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTteveNFPGF--TEGIMGPELmQNMREQAEKFgael 83
Cdd:PRK12775 427 SKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQY----GIPSFrlPRDIIDREV-QRLVDIGVKI---- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 84 rmelvtkvELEGDVKKIWVDDQEFQAR---TVILATGS-APRYLGVEGEqtLLGRGVSA--------CATCDGFFFRD-- 149
Cdd:PRK12775 498 --------ETNKVIGKTFTVPQLMNDKgfdAVFLGVGAgAPTFLGIPGE--FAGQVYSAnefltrvnLMGGDKFPFLDtp 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 150 ----HHIAVIGGGDSAMEEADFLTKFGS-KVSIIHRRDEFRASAIMLE-RAKNNPKIEFVTNKTVSKVLGDT--TVSGLE 221
Cdd:PRK12775 568 islgKSVVVIGAGNTAMDCLRVAKRLGApTVRCVYRRSEAEAPARIEEiRHAKEEGIDFFFLHSPVEIYVDAegSVRGMK 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 222 LTDTV--------------TGETSVLEATAMFVAIGHDPRSamfrdVVTTDAAGYVV----------VEHPSTK-TNVPG 276
Cdd:PRK12775 648 VEEMElgepdekgrrkpmpTGEFKDLECDTVIYALGTKANP-----IITQSTPGLALnkwgniaaddGKLESTQsTNLPG 722
|
330 340 350
....*....|....*....|....*....|...
gi 1437404552 277 VFAVGDLVDNHyQQAITAAGSGCRGAIDAEHYL 309
Cdd:PRK12775 723 VFAGGDIVTGG-ATVILAMGAGRRAARSIATYL 754
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
11-284 |
9.39e-10 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 59.17 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFE-------GIEYGGslmTTTEVENFPGfTEGIMGPELMQNMREQAEKFGAEL 83
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGG---TCLNVGCIPS-KALLASSEEFENAGHHFADHGIHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 84 ---------------------------------------RMELVTKVELEGDVKKIWVDDQEFQARTVILATGSAPRYL- 123
Cdd:PRK06327 82 dgvkidvakmiarkdkvvkkmtggieglfkknkitvlkgRGSFVGKTDAGYEIKVTGEDETVITAKHVIIATGSEPRHLp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 124 --GVEGEQTLLGRGVSACATCDGfffrdhHIAVIGGGDSAMEEADFLTKFGSKVSIIHRRDEFRASA---IMLERAKNNP 198
Cdd:PRK06327 162 gvPFDNKIILDNTGALNFTEVPK------KLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAAdeqVAKEAAKAFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 199 K--IEFVTNKTVSKVlgDTTVSGLELTDT-VTGETSVLEATAMFVAIGhdpRSAMFRDV------VTTDAAGYVVVEHpS 269
Cdd:PRK06327 236 KqgLDIHLGVKIGEI--KTGGKGVSVAYTdADGEAQTLEVDKLIVSIG---RVPNTDGLgleavgLKLDERGFIPVDD-H 309
|
330
....*....|....*
gi 1437404552 270 TKTNVPGVFAVGDLV 284
Cdd:PRK06327 310 CRTNVPNVYAIGDVV 324
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
105-285 |
2.77e-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: 57.68 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 105 QEFQARTVILATGSAPRYLGVEgeqtllgrGVSACATCDGFFFRDH---HIAVIGGGDSAMEEADFLTKF---GSKVSII 178
Cdd:TIGR01423 148 ERLQAEHILLATGSWPQMLGIP--------GIEHCISSNEAFYLDEpprRVLTVGGGFISVEFAGIFNAYkprGGKVTLC 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 179 HRRD--------EFRASAIMLERAKNnpkIEFVTNKTVSKVLGDTtvsglELTDTVTGET-SVLEATAMFVAIGHDPRSA 249
Cdd:TIGR01423 220 YRNNmilrgfdsTLRKELTKQLRANG---INIMTNENPAKVTLNA-----DGSKHVTFESgKTLDVDVVMMAIGRVPRTQ 291
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1437404552 250 MFR----DVVTTDAAGYVVVEHpsTKTNVPGVFAVGDLVD 285
Cdd:TIGR01423 292 TLQldkvGVELTKKGAIQVDEF--SRTNVPNIYAIGDVTD 329
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
73-284 |
3.49e-09 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 57.06 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 73 REQAEKFGAELRMELVTKVELEGdvKKIWVDD-QEFQARTVILATGSAPRYLGVEGeqtlLGR-GVSACATCDGFFFRDH 150
Cdd:COG1252 63 RELLRRAGVRFIQGEVTGIDPEA--RTVTLADgRTLSYDYLVIATGSVTNFFGIPG----LAEhALPLKTLEDALALRER 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 151 --------------HIAVIGGGDS----AMEEADFLTKFGS---------KVSIIHRRDEF------RASAIMLERAKNN 197
Cdd:COG1252 137 llaaferaerrrllTIVVVGGGPTgvelAGELAELLRKLLRypgidpdkvRITLVEAGPRIlpglgeKLSEAAEKELEKR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 198 pKIEFVTNKTVSKVLGDttvsGLELTDtvtGETsvLEATAMFVAIGHDPrSAMFRDV-VTTDAAGYVVVE----HPStkt 272
Cdd:COG1252 217 -GVEVHTGTRVTEVDAD----GVTLED---GEE--IPADTVIWAAGVKA-PPLLADLgLPTDRRGRVLVDptlqVPG--- 282
|
250
....*....|..
gi 1437404552 273 nVPGVFAVGDLV 284
Cdd:COG1252 283 -HPNVFAIGDCA 293
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
4-181 |
2.48e-08 |
|
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: 54.87 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 4 TTAGTIHDVAIIGSGPAGYTAALYAARAELKPIVFE-GIEYGG--------SLMTTTEV-------ENFPGFTEGIM-GP 66
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEkADDVGGtwrdnrypGLRLDTPShlyslpfFPNWSDDPDFPtGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 67 ELMQNMREQAEKFGAELRMEL---VTKVELEgDVKKIWV----DDQEFQARTVILATG--SAPRYLGVEGEQTLLGRGVS 137
Cdd:COG2072 81 EILAYLEAYADKFGLRRPIRFgteVTSARWD-EADGRWTvttdDGETLTARFVVVATGplSRPKIPDIPGLEDFAGEQLH 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1437404552 138 ACATCDGFFFRDHHIAVIGGGDSAMEEADFLTKFGSKVSIIHRR 181
Cdd:COG2072 160 SADWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
103-283 |
2.61e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 54.76 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 103 DDQEFQARTVILATGSAPRYLGVEGEQTLLG----RGVSACATcdgfffRDHHIAVIGGGDSAMEEADFLTKFGSKVSII 178
Cdd:PRK07251 113 EKIELTAETIVINTGAVSNVLPIPGLADSKHvydsTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 179 HRRDEF--RASAIMLERAKN---NPKIEFVTNKTVSKVLGDttvsGLELTDTVTGETSVLEatAMFVAIGHDPRSAMFR- 252
Cdd:PRK07251 187 DAASTIlpREEPSVAALAKQymeEDGITFLLNAHTTEVKND----GDQVLVVTEDETYRFD--ALLYATGRKPNTEPLGl 260
|
170 180 190
....*....|....*....|....*....|....
gi 1437404552 253 ---DVVTTDAAGYVVVEHpsTKTNVPGVFAVGDL 283
Cdd:PRK07251 261 entDIELTERGAIKVDDY--CQTSVPGVFAVGDV 292
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
151-313 |
6.30e-08 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 53.62 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 151 HIAVIGGGDSAMEEADFLTKFGSKVSIIHRRDEFrasaimlerAKNNPKI-EFVTN---KTVSKVLGDTTVSGLELTD-- 224
Cdd:PRK13748 272 RLAVIGSSVVALELAQAFARLGSKVTILARSTLF---------FREDPAIgEAVTAafrAEGIEVLEHTQASQVAHVDge 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 225 -TVTGETSVLEATAMFVAIGHDPRS---AMFRDVVTTDAAGYVVVEHpSTKTNVPGVFAVGDLVDNHyQQAITAAGSGCR 300
Cdd:PRK13748 343 fVLTTGHGELRADKLLVATGRAPNTrslALDAAGVTVNAQGAIVIDQ-GMRTSVPHIYAAGDCTDQP-QFVYVAAAAGTR 420
|
170
....*....|...
gi 1437404552 301 GAIDAEHYLAALN 313
Cdd:PRK13748 421 AAINMTGGDAALD 433
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
103-292 |
1.30e-07 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 52.70 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 103 DDQEFQARTVILATGSAPRYLGVEGEQTLLgrgvsacaTCDGFFF--RDHHIAVIGGGDSAMEEADFLTKFGSKVSIIHR 180
Cdd:PTZ00058 197 DGQVIEGKNILIAVGNKPIFPDVKGKEFTI--------SSDDFFKikEAKRIGIAGSGYIAVELINVVNRLGAESYIFAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 181 R-------DEFRASAIMLERAKNNPKIefVTNKTVSKVlgdTTVSGLELTDTVTGETSVLEATAMFVAIGHDPRSAMF-- 251
Cdd:PTZ00058 269 GnrllrkfDETIINELENDMKKNNINI--ITHANVEEI---EKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLnl 343
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1437404552 252 RDVVTTDAAGYVVVEHpSTKTNVPGVFAVGDLVDNHYQQAI 292
Cdd:PTZ00058 344 KALNIKTPKGYIKVDD-NQRTSVKHIYAVGDCCMVKKNQEI 383
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
103-289 |
1.32e-07 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 52.65 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 103 DDQEFQARTVILATGSAPRYLGVEGEQtllgrGVsacatcdGFFFRD---------HHIAVIGGGDSAMEEADFLTKFGS 173
Cdd:PRK07846 123 DGEEITADQVVIAAGSRPVIPPVIADS-----GV-------RYHTSDtimrlpelpESLVIVGGGFIAAEFAHVFSALGV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 174 KVSIIHRrdefraSAIMLeRAKNNPKIEFVTNKTVSKV---LGDTTVSGLELTDTVTGET---SVLEATAMFVAIGHDPR 247
Cdd:PRK07846 191 RVTVVNR------SGRLL-RHLDDDISERFTELASKRWdvrLGRNVVGVSQDGSGVTLRLddgSTVEADVLLVATGRVPN 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1437404552 248 SAMFrDV----VTTDAAGYVVV-EHpsTKTNVPGVFAVGDlVDNHYQ 289
Cdd:PRK07846 264 GDLL-DAaaagVDVDEDGRVVVdEY--QRTSAEGVFALGD-VSSPYQ 306
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
111-299 |
1.41e-07 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 52.91 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 111 TVILATGSAPRYLGVEGEQTllgRGVSACAT---CDGFFFRDHHI---AVIGGGDSAMEEADFLTKFGSKVSIIH----- 179
Cdd:TIGR02374 99 KLILATGSYPFILPIPGADK---KGVYVFRTiedLDAIMAMAQRFkkaAVIGGGLLGLEAAVGLQNLGMDVSVIHhapgl 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 180 -RRDEFRASAIMLERAKNNPKIEFVTNKTVSKVLGDTTVSGLELTDtvtgeTSVLEATAMFVAIGHDPRSAMFRDVVTTD 258
Cdd:TIGR02374 176 mAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKD-----GSSLEADLIVMAAGIRPNDELAVSAGIKV 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1437404552 259 AAGYVVveHPSTKTNVPGVFAVGD----------LVDNHYQQAITAAGSGC 299
Cdd:TIGR02374 251 NRGIIV--NDSMQTSDPDIYAVGEcaehngrvygLVAPLYEQAKVLADHIC 299
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
104-307 |
2.62e-07 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 51.71 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 104 DQEFQAR--TVILATGSAPRYLGVEGEQTLLGRGVSACATCDGFFFRDH--HIAVIGGGDSAMEEADFLTKFGSKVSIIH 179
Cdd:PRK13512 99 NEQFEESydKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQvdKALVVGAGYISLEVLENLYERGLHPTLIH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 180 RRDEFRAsaiMLERAKNNP--------KIEFVTNKTVSKVLGDTtvsgleltdtVTGETSVLEATAMFV-AIGHDPRSAM 250
Cdd:PRK13512 179 RSDKINK---LMDADMNQPildeldkrEIPYRLNEEIDAINGNE----------VTFKSGKVEHYDMIIeGVGTHPNSKF 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437404552 251 FRDV-VTTDAAGYVVVEHpSTKTNVPGVFAVGDLVDNHYQQA-----ITAAGSGCRGA-IDAEH 307
Cdd:PRK13512 246 IESSnIKLDDKGFIPVND-KFETNVPNIYAIGDIITSHYRHVdlpasVPLAWGAHRAAsIVAEQ 308
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
12-282 |
2.07e-06 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 49.09 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAAR--AELKPIVFEGIeyGGSLMTTTEVenfPGFTEgIMGPELMQNMREqAEKFGAELRMELVT 89
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQlgADVTVIERDGL--GGAAVLTDCV---PSKTL-IATAEVRTELRR-AAELGIRFIDDGEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 90 KVELE--------------GDVK-------------------------KIWVDD-----QEFQARTVILATGSAPRYLgv 125
Cdd:PRK07845 77 RVDLPavnarvkalaaaqsADIRarleregvrviagrgrlidpglgphRVKVTTadggeETLDADVVLIATGASPRIL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 126 egeqtllgrgvsACATCDG---FFFRD--------HHIAVIGGGDSAMEEADFLTKFGSKVSIIHRRD-----EFRASAI 189
Cdd:PRK07845 155 ------------PTAEPDGeriLTWRQlydldelpEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDrvlpgEDADAAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 190 MLERAKNNPKIEFVTNKTVSKV--LGDTTVSGLELTDTVTGeTSVLeatamfVAIGHDPRSA---MFRDVVTTDAAGYVV 264
Cdd:PRK07845 223 VLEEVFARRGMTVLKRSRAESVerTGDGVVVTLTDGRTVEG-SHAL------MAVGSVPNTAglgLEEAGVELTPSGHIT 295
|
330
....*....|....*...
gi 1437404552 265 VEHPStKTNVPGVFAVGD 282
Cdd:PRK07845 296 VDRVS-RTSVPGIYAAGD 312
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
12-57 |
4.83e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 47.57 E-value: 4.83e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1437404552 12 VAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTTEVENFP 57
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLP 47
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
18-128 |
7.42e-06 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 46.50 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 18 GPAGYTAALYAARAELKPIVFEGIEY------GGSLMTTT-----------EVEN--------FPGFTEGIMGP------ 66
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFpgdkicGGGLLPRAleeleplgldePLERpvrgarfySPGGKSVELPPgrgggy 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437404552 67 -----ELMQNMREQAEKFGAELRME-LVTKVELEGDvkKIWV---DDQEFQARTVILATGSA---PRYLGVEGE 128
Cdd:COG0644 82 vvdraRFDRWLAEQAEEAGAEVRTGtRVTDVLRDDG--RVVVrtgDGEEIRADYVVDADGARsllARKLGLKRR 153
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
10-57 |
1.99e-05 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 45.98 E-value: 1.99e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGSLMTTTEVENFP 57
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFR 49
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
6-120 |
4.43e-05 |
|
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: 44.42 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 6 AGTIHDVAIIGSGPAGYTAALYAARAELKPIVfegIEYGGSLMTTTEVEnfpgftegiMGPELMQNMREQaekfGAELRM 85
Cdd:COG0446 121 EFKGKRAVVIGGGPIGLELAEALRKRGLKVTL---VERAPRLLGVLDPE---------MAALLEEELREH----GVELRL 184
|
90 100 110
....*....|....*....|....*....|....*.
gi 1437404552 86 -ELVTKVELEGDVKKIWVDDQEFQARTVILATGSAP 120
Cdd:COG0446 185 gETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVRP 220
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
10-45 |
4.63e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 44.73 E-value: 4.63e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGG 45
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVG 52
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
12-282 |
7.15e-05 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 44.26 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 12 VAIIGSGPAGYTAALYAAR--AELKPIVFEgieyggslmtTTEVENF-----PGFTEGIM-GPELM-QNMREQAEKFGAE 82
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRlnKELEITVYE----------KTDIVSFgacglPYFVGGFFdDPNTMiARTPEEFIKSGID 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 83 LRMEL-VTKVELEGdvKKIWVDDQ----EFQAR--TVILATGSAPRYLGVEGEQTllgRGVSACATC-DGFFFRD----- 149
Cdd:PRK09564 73 VKTEHeVVKVDAKN--KTITVKNLktgsIFNDTydKLMIATGARPIIPPIKNINL---ENVYTLKSMeDGLALKEllkde 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 150 --HHIAVIGGGDSAMEEADFLTKFGSKVSIIHRRD---------EFraSAIMLERAKNNpKIEFVTNKTVSKVLGDTTVS 218
Cdd:PRK09564 148 eiKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDrilpdsfdkEI--TDVMEEELREN-GVELHLNEFVKSLIGEDKVE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437404552 219 GLEltdTVTGEtsvLEATAMFVAIGHDPRSAMFRDV-VTTDAAGYVVVEHpSTKTNVPGVFAVGD 282
Cdd:PRK09564 225 GVV---TDKGE---YEADVVIVATGVKPNTEFLEDTgLKTLKNGAIIVDE-YGETSIENIYAAGD 282
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
11-46 |
1.02e-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: 43.43 E-value: 1.02e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEGIEYGGS 46
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
11-118 |
1.69e-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: 42.69 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEGIEYG-----GSLMTTTEVENFPgftegIMGPELMQNMR------------ 73
Cdd:TIGR02032 2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPrykpcGGALSPRALEELD-----LPGELIVNLVRgarffspngdsv 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 74 ----------------------EQAEKFGAELRME-LVTKVELEGDVKKIWVDDQ--EFQARTVILATGS 118
Cdd:TIGR02032 77 eipietelayvidrdafdeqlaERAQEAGAELRLGtRVLDVEIHDDRVVVIVRGSegTVTAKIVIGADGS 146
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
11-48 |
1.96e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 42.95 E-value: 1.96e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEG----------IEYGGSLM 48
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEAdpvvggisrtVTYKGNRF 53
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
10-121 |
2.25e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 42.57 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFEG---------IEYGGSLMTT---TEVENF-------PGF----------- 59
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKgkklgrkilISGGGRCNVTnlsEEPDNFlsrypgnPKFlksalsrftpw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 60 ----------------TEGIMGP------ELMQNMREQAEKFGAELRMEL-VTKVELEGD-VKKIWVDDQEFQARTVILA 115
Cdd:pfam03486 81 dfiaffeslgvplkeeDHGRLFPdsdkasDIVDALLNELKELGVKIRLRTrVLSVEKDDDgRFRVKTGGEELEADSLVLA 160
|
....*...
gi 1437404552 116 TG--SAPR 121
Cdd:pfam03486 161 TGglSWPK 168
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
10-121 |
2.86e-04 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 42.13 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFE-------------------------------------------------- 39
Cdd:COG1053 4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqgginaagtnvqkaagedspeehfydtvkggdgladqd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 40 -------------------GIEYggSLMTTTEVENFPGFTEG-------IMGPELMQNMREQAEKFGAELRME-----LV 88
Cdd:COG1053 84 lvealaeeapeaidwleaqGVPF--SRTPDGRLPQFGGHSVGrtcyagdGTGHALLATLYQAALRLGVEIFTEtevldLI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1437404552 89 TKvelEGDVKKIWVDDQ-----EFQARTVILATGSAPR 121
Cdd:COG1053 162 VD---DGRVVGVVARDRtgeivRIRAKAVVLATGGFGR 196
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
10-60 |
4.22e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 41.76 E-value: 4.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFE-GIEYGGSLMTttevENFPGFT 60
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEkNDTPGGRART----FERPGFR 51
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
11-46 |
1.15e-03 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 40.40 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEGIE-YGGS 46
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPhYGGS 45
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
105-285 |
1.38e-03 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 40.18 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 105 QEFQARTVILATGSAPRYLGVEGEQTllgrgvsACATCDGFFFRD--HHIAVIGGGDSAMEEADFLTKFGSKVSIIHRR- 181
Cdd:PLN02507 164 LRYTAKHILIATGSRAQRPNIPGKEL-------AITSDEALSLEElpKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKe 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 182 -------DEFRAsaiMLERAKNNPKIEFVTNKTVSKVlgDTTVSGLELTdTVTGETsvLEATAMFVAIGHDPRSAM--FR 252
Cdd:PLN02507 237 lplrgfdDEMRA---VVARNLEGRGINLHPRTNLTQL--TKTEGGIKVI-TDHGEE--FVADVVLFATGRAPNTKRlnLE 308
|
170 180 190
....*....|....*....|....*....|....
gi 1437404552 253 DV-VTTDAAGYVVVEHPStKTNVPGVFAVGDLVD 285
Cdd:PLN02507 309 AVgVELDKAGAVKVDEYS-RTNIPSIWAIGDVTN 341
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
11-75 |
1.54e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 39.90 E-value: 1.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFEgiEYG--GSLMTTTEVENFPGFTE-------GIMGpELMQNMREQ 75
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVE--RRGflGGMLTSGLVGPDMGFYLnkeqvvgGIAR-EFRQRLRAR 71
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
11-46 |
3.03e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 39.02 E-value: 3.03e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1437404552 11 DVAIIGSGPAGYTAALYAARAELKPIVFE-GIEYGGS 46
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEkSAHFGGS 49
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
148-283 |
3.37e-03 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 38.84 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 148 RDHHIAVIGGGDSAMEEADFLTKFGSKVSIIHRRDEF-----RASAIMLERAKNNPKIEFVTNKTVSKvlgdttVSGLEL 222
Cdd:PRK08010 157 LPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFlpredRDIADNIATILRDQGVDIILNAHVER------ISHHEN 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437404552 223 TDTVTGETSVLEATAMFVAIGHDPRSAMFR----DVVTTDAAGYVVVEHPSTKTNvpGVFAVGDL 283
Cdd:PRK08010 231 QVQVHSEHAQLAVDALLIASGRQPATASLHpenaGIAVNERGAIVVDKYLHTTAD--NIWAMGDV 293
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
1-84 |
5.08e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 38.36 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 1 MTDTTAGTihDVAIIGSGPAGYTAALYAARAELKPIVFEGIEY-GGSLMTTTeVENFPGFTEgiMGPEL----MQNMREQ 75
Cdd:COG1231 1 MSRRARGK--DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRvGGRVWTLR-FGDDGLYAE--LGAMRippsHTNLLAL 75
|
....*....
gi 1437404552 76 AEKFGAELR 84
Cdd:COG1231 76 ARELGLPLE 84
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
165-264 |
5.25e-03 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 38.09 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437404552 165 ADFLTKFGSKVSIIHRRDefrASAIMLERAKNNPKIEFVTNKTVSKVLGDTTvsGLELTDTvtgETSVLEATAMfvaIGH 244
Cdd:PRK08163 93 QAFRARFGNPYAVIHRAD---IHLSLLEAVLDHPLVEFRTSTHVVGIEQDGD--GVTVFDQ---QGNRWTGDAL---IGC 161
|
90 100
....*....|....*....|...
gi 1437404552 245 DPRSAMFRDVVTTDAA---GYVV 264
Cdd:PRK08163 162 DGVKSVVRQSLVGDAPrvtGHVV 184
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
10-39 |
7.76e-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: 37.61 E-value: 7.76e-03
10 20 30
....*....|....*....|....*....|
gi 1437404552 10 HDVAIIGSGPAGYTAALYAARAELKPIVFE 39
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVE 33
|
|
| |
