|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
2-300 |
2.10e-147 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 416.06 E-value: 2.10e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNTSDIENYPGY-DLISGPELSMKMHEPLEKFGVENLYGIVT 80
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFpEGISGPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 81 AVEDHGNFKKVLTDD-NSYETKTVIIATGAKHRPLAVAGEETYNSRGVSYCAVCDGAFFRGQDLLVVGGGDSAVEEALFL 159
Cdd:COG0492 81 SVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 160 TRFANKVTIVHRRDELRAQKVLQERAFANDKVDFIWNSVVKEIKGNDlKVTNVDIENVKTGQVNNYAFGGVFIYVGLDPV 239
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVKTGEEKELEVDGVFVAIGLKPN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518635133 240 SSMVKELDI-TDEAGWIPTDDHMKTKAAGVFAIGDVRQKDLRQITTAVGDGAVAAQEAYQYI 300
Cdd:COG0492 240 TELLKGLGLeLDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
3-300 |
1.02e-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: 393.92 E-value: 1.02e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 3 DTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNTSDIENYPGY-DLISGPELSMKMHEPLEKFGVENLYGIVTA 81
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFpEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 82 VEDHGNFKKVLTDDNS-YETKTVIIATGAKHRPLAVAGEETYNSRGVSYCAVCDGAFFRGQDLLVVGGGDSAVEEALFLT 160
Cdd:TIGR01292 81 VDKSDRPFKVYTGDGKeYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 161 RFANKVTIVHRRDELRAQKVLQERAFANDKVDFIWNSVVKEIKGNDlKVTNVDIENVKTGQVNNYAFGGVFIYVGLDPVS 240
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDN-KVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 241 SMVKELDITDEAGWIPTDDHMKTKAAGVFAIGDVRQKDLRQITTAVGDGAVAAQEAYQYI 300
Cdd:TIGR01292 240 ELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
1-301 |
1.30e-98 |
|
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: 300.54 E-value: 1.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNTSDIENYPGYDLISGPELSMKMHEPLEKFGVENLYGIVT 80
Cdd:TIGR03143 4 IYDLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQAEVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 81 AVEDHGNFKKVLTDDNSYETKTVIIATGAKHRPLAVAGEETYNSRGVSYCAVCDGAFFRGQDLLVVGGGDSAVEEALFLT 160
Cdd:TIGR03143 84 DVDFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 161 RFANKVTIVHRRDELRAQKVLQERAFANDKVDFIWNSVVKEIKGNDlKVTNVDIENVKTGQVNNY-------AFgGVFIY 233
Cdd:TIGR03143 164 RYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDD-GLRYAKFVNNVTGEITEYkapkdagTF-GVFVF 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518635133 234 VGLDPVSSMVKELDITDEAGWIPTDDHMKTKAAGVFAIGDVRQKDLRQITTAVGDGAVAAQEAYQYIV 301
Cdd:TIGR03143 242 VGYAPSSELFKGVVELDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVK 309
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
2-303 |
4.75e-68 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 220.42 E-value: 4.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIeqgAP--GGQMNNTSDIENYPGYDLISGPELSMKMHEPLEKFGVENLYGI- 78
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIV---AErfGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQr 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 79 VTAVEDHGNFKKV-LTDDNSYETKTVIIATGAKHRPLAVAGEETYNSRGVSYCAVCDGAFFRGQDLLVVGGGDSAVEEAL 157
Cdd:PRK15317 289 ASKLEPAAGLIEVeLANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAI 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 158 FLTRFANKVTIVHRRDELRAQKVLQERAFANDKVDFIWNSVVKEIKGNDLKVTNVDIENVKTGQVNNYAFGGVFIYVGLD 237
Cdd:PRK15317 369 DLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLV 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518635133 238 PVSSMVKELDITDEAGWIPTDDHMKTKAAGVFAIGDVRQKDLRQITTAVGDGAVAAQEAYQYIVNN 303
Cdd:PRK15317 449 PNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYLIRN 514
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
5-300 |
3.88e-60 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 194.51 E-value: 3.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 5 IIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNTSDIENYPG-YDLISGPELSMKMHEPLEKFGVENLYGIVTAVE 83
Cdd:PRK10262 10 LILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGdPNDLTGPLLMERMHEHATKFETEIIFDHINKVD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 84 DHGNFKKVLTDDNSYETKTVIIATGAKHRPLAVAGEETYNSRGVSYCAVCDGAFFRGQDLLVVGGGDSAVEEALFLTRFA 163
Cdd:PRK10262 90 LQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 164 NKVTIVHRRDELRAQKVLQERAF---ANDKVDFIWNSVVKEIKGNDLKVTNVDIENVK-TGQVNNYAFGGVFIYVGLDPv 239
Cdd:PRK10262 170 SEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQnSDNIESLDVAGLFVAIGHSP- 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518635133 240 SSMVKELDITDEAGWIPTD-----DHMKTKAAGVFAIGDVRQKDLRQITTAVGDGAVAAQEAYQYI 300
Cdd:PRK10262 249 NTAIFEGQLELENGYIKVQsgihgNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
2-289 |
4.42e-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: 185.98 E-value: 4.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGA--PGGQMNNTSDIENY--PGYDLISGPELSMKMHEPLEKF--GVENL 75
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGtcPYGGCVLSKALLGAaeAPEIASLWADLYKRKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 76 YGI-VTAVE-DHGNFK---KVLTDDNSYETKTVIIATGAKHRPLAVAGEETYNSRGVSYCAVCDGAFF--RGQDLLVVGG 148
Cdd:pfam07992 81 LGTeVVSIDpGAKKVVleeLVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLklLPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 149 GDSAVEEALFLTRFANKVTIVHRRDEL------RAQKVLQERaFANDKVDFIWNSVVKEIKGNDLKVTnvdienVKTGQV 222
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKA-LEKNGVEVRLGTSVKEIIGDGDGVE------VILKDG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518635133 223 NNYAFGGVFIYVGLDPVSSMVKELDI-TDEAGWIPTDDHMKTKAAGVFAIGDVRQKDLRQITTAVGDG 289
Cdd:pfam07992 234 TEIDADLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-274 |
3.79e-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: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGG------------------QMNNTSDIENYpGYDlISGPELSM- 61
Cdd:COG1249 3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGtclnvgcipskallhaaeVAHEARHAAEF-GIS-AGAPSVDWa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 62 KMHEPLEKFgVENLYGI---------VTAVEDHGNFKK----VLTDDNSYETKTVIIATGAKHRPLAVAGEEtyNSRGVS 128
Cdd:COG1249 81 ALMARKDKV-VDRLRGGveellkkngVDVIRGRARFVDphtvEVTGGETLTADHIVIATGSRPRVPPIPGLD--EVRVLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 129 YcavcDGAF---FRGQDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDEL------RAQKVLQeRAFANDKVDFIWNSVV 199
Cdd:COG1249 158 S----DEALeleELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpgedpEISEALE-KALEKEGIDILTGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 200 KEIKGNDLKVTnVDIENVKTGQVnnYAFGGVFIYVGLDPVssmVKELDI------TDEAGWIPTDDHMKTKAAGVFAIGD 273
Cdd:COG1249 233 TSVEKTGDGVT-VTLEDGGGEEA--VEADKVLVATGRRPN---TDGLGLeaagveLDERGGIKVDEYLRTSVPGIYAIGD 306
|
.
gi 518635133 274 V 274
Cdd:COG1249 307 V 307
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-274 |
7.76e-27 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 109.11 E-value: 7.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGG---------------QMNNTSDIENYPGYDL-ISGPELSMK-- 62
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGtclnvgcipskaliaAAEAFHEAKHAEEFGIhADGPKIDFKkv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 63 --------------MHEPLEKFGVENLY-GIVTAVEDHgnfkKVLTDDNSYETKTVIIATGAkhRPLAVAGEETYNSRG- 126
Cdd:PRK06292 83 marvrrerdrfvggVVEGLEKKPKIDKIkGTARFVDPN----TVEVNGERIEAKNIVIATGS--RVPPIPGVWLILGDRl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 127 VSYcavcDGAFFR---GQDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDEL----------RAQKVLQERafandkVDF 193
Cdd:PRK06292 157 LTS----DDAFELdklPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE------FKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 194 IWNSVVKEI-KGNDLKVTNVDIE-NVKTGQVNNyafggVFIYVGLDPVSSM--VKELDI-TDEAGWIPTDDHMKTKAAGV 268
Cdd:PRK06292 227 KLGAKVTSVeKSGDEKVEELEKGgKTETIEADY-----VLVATGRRPNTDGlgLENTGIeLDERGRPVVDEHTQTSVPGI 301
|
....*.
gi 518635133 269 FAIGDV 274
Cdd:PRK06292 302 YAAGDV 307
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
1-277 |
1.38e-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: 108.50 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNTSDI---------ENYPGYD-------LISGPELSM-KM 63
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIptkallhsaEVYDEIKhakdlgiEVENVSVDWeKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 64 HEPLEKF------GVENLY--GIVTAVEDHGNFKK----VLTDDN---SYETKTVIIATGAKHR----PLAVAGEETYNS 124
Cdd:TIGR01350 81 QKRKNKVvkklvgGVSGLLkkNKVTVIKGEAKFLDpgtvSVTGENgeeTLEAKNIIIATGSRPRslpgPFDFDGKVVITS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 125 rgvsycavcDGAF-FRG--QDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDELRAQ------KVLQeRAFANDKVDFIW 195
Cdd:TIGR01350 161 ---------TGALnLEEvpESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGedaevsKVLQ-KALKKKGVKILT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 196 NSVVKEIKGNDLKVTnvdIENVKtGQVNNYAFGGVFIYVGLDPVSSM--VKELDI-TDEAGWIPTDDHMKTKAAGVFAIG 272
Cdd:TIGR01350 231 NTKVTAVEKNDDQVT---YENKG-GETETLTGEKVLVAVGRKPNTEGlgLEKLGVeLDERGRIVVDEYMRTNVPGIYAIG 306
|
....*
gi 518635133 273 DVRQK 277
Cdd:TIGR01350 307 DVIGG 311
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
6-304 |
3.05e-19 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 87.54 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIE-QGAPGGQmnNTSDIenyPGYDLisgP-ELSMKMHEPLEKFGVEnlygIVTave 83
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTIFEaRDKAGGL--LRYGI---PEFRL---PkDIVDREVERLLKLGVE----IRT--- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 84 dhgNFK--KVLT-DDNSYETKTVIIATGA-KHRPLAVAGEetyNSRGVsYCAV----------CDGAFFRGQDLLVVGGG 149
Cdd:PRK11749 210 ---NTEvgRDITlDELRAGYDAVFIGTGAgLPRFLGIPGE---NLGGV-YSAVdfltrvnqavADYDLPVGKRVVVIGGG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 150 DSAVEEALFLTRF-ANKVTIVHRRD--ELRAQKvlQERAFA-NDKVDFIWNSVVKEIKGNDLKVTNVDIENVKTGQVNny 225
Cdd:PRK11749 283 NTAMDAARTAKRLgAESVTIVYRRGreEMPASE--EEVEHAkEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELGEPD-- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 226 aFGG-----------------VFIYVGLDP---VSSMVKELDITDEAGWIPTDDHMKTKAAGVFAIGD-VRQKDLrqITT 284
Cdd:PRK11749 359 -ASGrrrvpiegseftlpadlVIKAIGQTPnplILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDiVTGAAT--VVW 435
|
330 340
....*....|....*....|
gi 518635133 285 AVGDGAVAAQEAYQYIVNNY 304
Cdd:PRK11749 436 AVGDGKDAAEAIHEYLEGAA 455
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
11-272 |
4.25e-18 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 82.66 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 11 PAGMTAALYAARSNLK-VALIEQGAPGgqmnNTsdIENYPgydlisgpeLSMKM---HEPLEKFGVENLYGI-------- 78
Cdd:pfam13738 1 PAGIGCAIALKKAGLEdYLILEKGNIG----NS--FYRYP---------THMTFfspSFTSNGFGIPDLNAIspgtspaf 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 79 --------------------------------VTAVEDHGNFKKVLTDDNSYETKTVIIATGAKHRPlAVAGEETYnsrG 126
Cdd:pfam13738 66 tfnrehpsgneyaeylrrvadhfelpinlfeeVTSVKKEDDGFVVTTSKGTYQARYVIIATGEFDFP-NKLGVPEL---P 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 127 VSYCAVCDGAFFRGQDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDELRAQK----------VLQ--ERAFANDKVDFI 194
Cdd:pfam13738 142 KHYSYVKDFHPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDsdpsyslspdTLNrlEELVKNGKIKAH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 195 WNSVVKEIKGNDLKVTnVDIENVKTGQVNNyafggVFIY-VGLDP-VSSMVKELDITDEAGWIP-TDDHMKTKAAGVFAI 271
Cdd:pfam13738 222 FNAEVKEITEVDVSYK-VHTEDGRKVTSND-----DPILaTGYHPdLSFLKKGLFELDEDGRPVlTEETESTNVPGLFLA 295
|
.
gi 518635133 272 G 272
Cdd:pfam13738 296 G 296
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-274 |
1.04e-17 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 82.89 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNTSDIenyPGYDLISGPELSMKMHEpLEKFG--------- 71
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCI---PSKALLHAAERADEARH-SEDFGikaenvgid 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 72 -----------VENLYG---------IVTAVEDHGNFK-----KVLTDDNS--YETKTVIIATGAkhRPLAVAGEETYNS 124
Cdd:PRK06416 80 fkkvqewkngvVNRLTGgvegllkknKVDIIRGEAKLVdpntvRVMTEDGEqtYTAKNIILATGS--RPRELPGIEIDGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 125 RGVSYcavcDGAF---FRGQDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDELRA------QKVLqERAFANDKVDFIW 195
Cdd:PRK06416 158 VIWTS----DEALnldEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPgedkeiSKLA-ERALKKRGIKIKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 196 NSVVKEIKGNDLKVTnVDIEnvKTGQVNNYAFGGVFIYVGLDPVSSMV--KELDITDEAGWIPTDDHMKTKAAGVFAIGD 273
Cdd:PRK06416 233 GAKAKKVEQTDDGVT-VTLE--DGGKEETLEADYVLVAVGRRPNTENLglEELGVKTDRGFIEVDEQLRTNVPNIYAIGD 309
|
.
gi 518635133 274 V 274
Cdd:PRK06416 310 I 310
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
24-274 |
2.37e-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: 77.93 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 24 NLKVALIEQGA-PGGQmnntsdieNYPGYDLISGP-----ELSMKMHEPLEKFGVE-NLYGIVTAVeDHGNfKKVLTDDN 96
Cdd:COG0446 5 DAEITVIEKGPhHSYQ--------PCGLPYYVGGGikdpeDLLVRTPESFERKGIDvRTGTEVTAI-DPEA-KTVTLRDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 97 ---SYETktVIIATGAKHRPLAVAGeetYNSRGVSYCAVCDGAF--------FRGQDLLVVGGGDSAVEEALFLTRFANK 165
Cdd:COG0446 75 etlSYDK--LVLATGARPRPPPIPG---LDLPGVFTLRTLDDADalrealkeFKGKRAVVIGGGPIGLELAEALRKRGLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 166 VTIVHRRDEL----------RAQKVLQERafandKVDFIWNSVVKEIKGNDlKVTnVDIENVKTgqvnnYAFGGVFIYVG 235
Cdd:COG0446 150 VTLVERAPRLlgvldpemaaLLEEELREH-----GVELRLGETVVAIDGDD-KVA-VTLTDGEE-----IPADLVVVAPG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518635133 236 LDPVSSMVKELDI-TDEAGWIPTDDHMKTKAAGVFAIGDV 274
Cdd:COG0446 218 VRPNTELAKDAGLaLGERGWIKVDETLQTSDPDVYAAGDC 257
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-212 |
1.32e-15 |
|
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: 70.31 E-value: 1.32e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518635133 143 LLVVGGGDSAVEEALFLTRFANKVTIVHRRDELR------AQKVLQERaFANDKVDFIWNSVVKEIKGNDLKVTNV 212
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEK-LEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
6-295 |
2.36e-15 |
|
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: 75.94 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIE-QGAPGGQMnnTSDIenyPGYDLisgP-ELSMKMHEPLEKFGVEnlygIVTAVE 83
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEaLDKPGGLL--RYGI---PEFRL---PkDVLDREIELIEALGVE----FRTNVE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 84 dhgnfkkvLTDDNSYET-----KTVIIATGA-KHRPLAVAGEEtynSRGVsYCAV-----------CDGAFFRGQDLLVV 146
Cdd:COG0493 194 --------VGKDITLDElleefDAVFLATGAgKPRDLGIPGED---LKGV-HSAMdfltavnlgeaPDTILAVGKRVVVI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 147 GGGDSAVEEALFLTRF-ANKVTIVHRRD--ELRAQKVLQERAFAnDKVDFIWNSVVKEIKGN-DLKVTNVDIENVK---- 218
Cdd:COG0493 262 GGGNTAMDCARTALRLgAESVTIVYRRTreEMPASKEEVEEALE-EGVEFLFLVAPVEIIGDeNGRVTGLECVRMElgep 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 219 --TGQVNNYAFGG---------VFIYVGLDPVSS-MVKELDI-TDEAGWIPTD-DHMKTKAAGVFAIGD-VRQKDLrqIT 283
Cdd:COG0493 341 deSGRRRPVPIEGseftlpadlVILAIGQTPDPSgLEEELGLeLDKRGTIVVDeETYQTSLPGVFAGGDaVRGPSL--VV 418
|
330
....*....|..
gi 518635133 284 TAVGDGAVAAQE 295
Cdd:COG0493 419 WAIAEGRKAARA 430
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
2-274 |
8.28e-14 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 71.50 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIE-------QGAPGGQMNNTSDIenyPGYDLISGPELSMKMHEPLEKFGVE- 73
Cdd:PRK06327 5 FDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCI---PSKALLASSEEFENAGHHFADHGIHv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 74 --------------------NLYGI--------VTAVEDHGNFK---------KVLTDDNS-YETKTVIIATGAKHRPLA 115
Cdd:PRK06327 82 dgvkidvakmiarkdkvvkkMTGGIeglfkknkITVLKGRGSFVgktdagyeiKVTGEDETvITAKHVIIATGSEPRHLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 116 VAGeetynsrgVSYCAVCD--GAFFRGQ---DLLVVGGGDSAVEEALFLTRFANKVTIVHRRDELRA---QKVLQE--RA 185
Cdd:PRK06327 162 GVP--------FDNKIILDntGALNFTEvpkKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAaadEQVAKEaaKA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 186 FANDKVDFIWNSVVKEIK--GNDLKVTNVDIE-NVKTGQVNNY--AFGGVFIYVGLDPVSSMVKeldiTDEAGWIPTDDH 260
Cdd:PRK06327 234 FTKQGLDIHLGVKIGEIKtgGKGVSVAYTDADgEAQTLEVDKLivSIGRVPNTDGLGLEAVGLK----LDERGFIPVDDH 309
|
330
....*....|....
gi 518635133 261 MKTKAAGVFAIGDV 274
Cdd:PRK06327 310 CRTNVPNVYAIGDV 323
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
6-293 |
6.17e-13 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 68.75 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIEQGA-PGGQMNntsdienY--PGYDLisgPElsmkmhEPLE-------KFGVENL 75
Cdd:PRK12771 142 VIGGGPAGLSAAYHLRRMGHAVTIFEAGPkLGGMMR-------YgiPAYRL---PR------EVLDaeiqrilDLGVEVR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 76 YGiVTAVEDhgnfkkVLTDDNSYETKTVIIATGA-KHRPLAVAGEETYN-SRGVSYC-AVCDG-AFFRGQDLLVVGGGDS 151
Cdd:PRK12771 206 LG-VRVGED------ITLEQLEGEFDAVFVAIGAqLGKRLPIPGEDAAGvLDAVDFLrAVGEGePPFLGKRVVVIGGGNT 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 152 AVEEALFLTRF-ANKVTIVHRR--DELRAQKVLQERAFAnDKVDFIWNSVVKEIKGNDLKVTNVDIENVKTGQVN----N 224
Cdd:PRK12771 279 AMDAARTARRLgAEEVTIVYRRtrEDMPAHDEEIEEALR-EGVEINWLRTPVEIEGDENGATGLRVITVEKMELDedgrP 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 225 YAFGGVFIYVGLDPV---------SSMVKELD-ITDEAGWIPTDDH-MKTKAAGVFAIGDVrQKDLRQITTAVGDGAVAA 293
Cdd:PRK12771 358 SPVTGEEETLEADLVvlaigqdidSAGLESVPgVEVGRGVVQVDPNfMMTGRPGVFAGGDM-VPGPRTVTTAIGHGKKAA 436
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
2-277 |
8.29e-13 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 68.31 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNT---------------SDIEN--YPGYDlISGP------- 57
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTgcvptktliasaraaHLARRaaEYGVS-VGGPvsvdfka 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 58 ------ELSMKMHEPLEKfGVENLYGiVTAVEDHGNF---KKVLTDDNSYETKTVIIATGAkhRPLA--VAGEETynsrg 126
Cdd:PRK06370 85 vmarkrRIRARSRHGSEQ-WLRGLEG-VDVFRGHARFespNTVRVGGETLRAKRIFINTGA--RAAIppIPGLDE----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 127 VSYCAvCDGAF---FRGQDLLVVGGGDSAVEEALFLTRFANKVTIVHR------RDELRAQKVLQErAFANDKVDFIWNS 197
Cdd:PRK06370 156 VGYLT-NETIFsldELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERgprllpREDEDVAAAVRE-ILEREGIDVRLNA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 198 VVKEIKGNDlkvTNVDIENVKTGQVNNYAFGGVFIYVGLDPvssMVKELDI------TDEAGWIPTDDHMKTKAAGVFAI 271
Cdd:PRK06370 234 ECIRVERDG---DGIAVGLDCNGGAPEITGSHILVAVGRVP---NTDDLGLeaagveTDARGYIKVDDQLRTTNPGIYAA 307
|
....*.
gi 518635133 272 GDVRQK 277
Cdd:PRK06370 308 GDCNGR 313
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
2-297 |
1.07e-11 |
|
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: 64.87 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAP---------GGQMNNTSDI-ENYPGYDLISGPELsmkmhEPLEKFG 71
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgiGGTCVNVGCIpKKLMHQAALLGQAL-----KDSRNYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 72 --VENLYG-----IVTAVEDH---GNF--------KKV--------------------LTDDNSYETKTVIIATGAKHRP 113
Cdd:TIGR01438 78 wkVEETVKhdwkrLVEAVQNHigsLNWgyrvalreKKVkyenayaefvdkhrikatnkKGKEKIYSAERFLIATGERPRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 114 LAVAGEEtynsrgvSYCAVCDGAFFRGQD---LLVVGGGDSAVEEALFLTRFANKVTIVHRRDELR------AQKV---L 181
Cdd:TIGR01438 158 PGIPGAK-------ELCITSDDLFSLPYCpgkTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRgfdqdcANKVgehM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 182 QERAfandkVDFIWNSVVKEIK--GNDLKVTNVDIENVKTGQVNN--YAFGGVFIYVGLDPVSSMVKeldITDEAGWIPT 257
Cdd:TIGR01438 231 EEHG-----VKFKRQFVPIKVEqiEAKVLVEFTDSTNGIEEEYDTvlLAIGRDACTRKLNLENVGVK---INKKTGKIPA 302
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 518635133 258 DDHMKTKAAGVFAIGDVRQKDLRQITTAVGDGAVAAQEAY 297
Cdd:TIGR01438 303 DEEEQTNVPYIYAVGDILEDKPELTPVAIQAGRLLAQRLF 342
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
2-274 |
1.08e-11 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 64.79 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNN---------------TSDIENY-PGY-------------- 51
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNvgcvpkklmwygaqiAEAFHDYaPGYgfdvtenkfdwakl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 52 --------DLISGPELSMkmhepLEKFGVENLYGIVTAVEDHgnfkKVLTDDNSYETKTVIIATGAKHRPLAVAGEEtyn 123
Cdd:PRK06116 85 ianrdayiDRLHGSYRNG-----LENNGVDLIEGFARFVDAH----TVEVNGERYTADHILIATGGRPSIPDIPGAE--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 124 srgvsYCAVCDGAFF---RGQDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDE-LRA-----QKVLQErAFANDKVDFI 194
Cdd:PRK06116 153 -----YGITSDGFFAleeLPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGfdpdiRETLVE-EMEKKGIRLH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 195 WNSVVKEIKGND---LKVTNVDIENVKTGQVnnyafggvfIY-VGLDPvssMVKELDI------TDEAGWIPTDDHMKTK 264
Cdd:PRK06116 227 TNAVPKAVEKNAdgsLTLTLEDGETLTVDCL---------IWaIGREP---NTDGLGLenagvkLNEKGYIIVDEYQNTN 294
|
330
....*....|
gi 518635133 265 AAGVFAIGDV 274
Cdd:PRK06116 295 VPGIYAVGDV 304
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1-274 |
5.68e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 62.46 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAAR---SNLKVALIEQgapggqmNNTSdieNYPG--YDLISGP----ELSMKMHEPLEKFG 71
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDP-------NPYH---LFQPllPEVAAGTlspdDIAIPLRELLRRAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 72 VENLYGIVTAVeDHGNfKKVLTDDN---SYETktVIIATGAKHRPLAVAGEETYnsrGVSYCAVCDGAFFRGQ------- 141
Cdd:COG1252 71 VRFIQGEVTGI-DPEA-RTVTLADGrtlSYDY--LVIATGSVTNFFGIPGLAEH---ALPLKTLEDALALRERllaafer 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 142 ----DLL---VVGGGDSAVEEALFLTRFANK-------------VTIVHRRDEL----------RAQKVLQERafandKV 191
Cdd:COG1252 144 aerrRLLtivVVGGGPTGVELAGELAELLRKllrypgidpdkvrITLVEAGPRIlpglgeklseAAEKELEKR-----GV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 192 DFIWNSVVKEIKGNdlKVTnvdienVKTGQVNNYAFggvFIYVGldPV--SSMVKELDI-TDEAGWIPTDDHMKTKA-AG 267
Cdd:COG1252 219 EVHTGTRVTEVDAD--GVT------LEDGEEIPADT---VIWAA--GVkaPPLLADLGLpTDRRGRVLVDPTLQVPGhPN 285
|
....*..
gi 518635133 268 VFAIGDV 274
Cdd:COG1252 286 VFAIGDC 292
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
6-293 |
6.04e-11 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 62.82 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIEQG-APGGQMNntsdiENYPGYDLisgPELSMKMH-EPLEKFGVENLYGIVTAve 83
Cdd:PRK12814 198 IIGAGPAGLTAAYYLLRKGHDVTIFDANeQAGGMMR-----YGIPRFRL---PESVIDADiAPLRAMGAEFRFNTVFG-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 84 dhgnfKKVLTDDNSYETKTVIIATGA-KHRPLAVAGEEtynSRGVsycaVCDGAFFR----------GQDLLVVGGGDSA 152
Cdd:PRK12814 268 -----RDITLEELQKEFDAVLLAVGAqKASKMGIPGEE---LPGV----ISGIDFLRnvalgtalhpGKKVVVIGGGNTA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 153 VEEALFLTRF-ANKVTIVHRR--DELRAQKVLQERAFANDKVDFIWNSVVKEIKGND-LKVTNVDI---ENVKTGQVNNY 225
Cdd:PRK12814 336 IDAARTALRLgAESVTILYRRtrEEMPANRAEIEEALAEGVSLRELAAPVSIERSEGgLELTAIKMqqgEPDESGRRRPV 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 226 AFGGVFIYVGLDPV-SSMVKELDI---------TDEAGWIPTDDH-MKTKAAGVFAIGD-VRQKDLrqITTAVGDGAVAA 293
Cdd:PRK12814 416 PVEGSEFTLQADTViSAIGQQVDPpiaeaagigTSRNGTVKVDPEtLQTSVAGVFAGGDcVTGADI--AINAVEQGKRAA 493
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1-274 |
9.31e-11 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 62.08 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAAlyaarsnlkVALIEQGAPGgqmnntsDI-----ENYPGYD------LISG--PELSMKMHEP- 66
Cdd:COG1251 1 KMRIVIIGAGMAGVRAA---------EELRKLDPDG-------EItvigaEPHPPYNrpplskVLAGetDEEDLLLRPAd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 67 -LEKFGVENLYGI-VTAVeDHGNfKKVLTDDN---SYETktVIIATGAKHRPLAVAGEE-----TYNSRgvsycAVCD-- 134
Cdd:COG1251 65 fYEENGIDLRLGTrVTAI-DRAA-RTVTLADGetlPYDK--LVLATGSRPRVPPIPGADlpgvfTLRTL-----DDADal 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 135 -GAFFRGQDLLVVGGGdsaveealFL-TRFAN-------KVTIVHRRDEL-------RAQKVLQeRAFANDKVDFIWNSV 198
Cdd:COG1251 136 rAALAPGKRVVVIGGG--------LIgLEAAAalrkrglEVTVVERAPRLlprqldeEAGALLQ-RLLEALGVEVRLGTG 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518635133 199 VKEIKGNDlKVTNVdieNVKTGQVnnYAFGGVFIYVGLDPVSSMVKELDITDEAGwIPTDDHMKTKAAGVFAIGDV 274
Cdd:COG1251 207 VTEIEGDD-RVTGV---RLADGEE--LPADLVVVAIGVRPNTELARAAGLAVDRG-IVVDDYLRTSDPDIYAAGDC 275
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
5-113 |
9.69e-11 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 61.84 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 5 IIIGSGPAGMTAALYAARSNLKVALIEQG---------APGGQMN--NTSDIE----NYPG--------------YDLIS 55
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNkkigkklliSGGGRCNltNSCPTPefvaYYPRngkflrsalsrfsnKDLID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 56 -----GPEL-----------SMK--------MHEpLEKFGVENLYGI-VTAVEDHGNFKKVLTDDNSYETKTVIIATGAK 110
Cdd:TIGR00275 81 ffeslGLELkveedgrvfpcSDSaadvldalLNE-LKELGVEILTNSkVKSIEKEDGGFGVETSGGEYEADKVIIATGGL 159
|
...
gi 518635133 111 HRP 113
Cdd:TIGR00275 160 SYP 162
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
2-274 |
9.97e-11 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 62.07 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAP--GGQMNNTSDIenyPGYDLISGPELSMKMHEPLEKFGV------- 72
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCI---PTKTLLVAAEKNLSFEQVMATKNTvtsrlrg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 73 ENLYGIVTAVED----HGNF--KKVL-----TDDNSYETKTVIIATGAKHRPLAVAG----EETYNSRGVSYCAVcdgaf 137
Cdd:PRK07251 81 KNYAMLAGSGVDlydaEAHFvsNKVIevqagDEKIELTAETIVINTGAVSNVLPIPGladsKHVYDSTGIQSLET----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 138 fRGQDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDEL--RAQKVLQERA---FANDKVDFIWNSVVKEIKGNDLKVtnv 212
Cdd:PRK07251 156 -LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTIlpREEPSVAALAkqyMEEDGITFLLNAHTTEVKNDGDQV--- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518635133 213 dienVKTGQVNNYAFGGVFIYVGLDPVSS--MVKELDI-TDEAGWIPTDDHMKTKAAGVFAIGDV 274
Cdd:PRK07251 232 ----LVVTEDETYRFDALLYATGRKPNTEplGLENTDIeLTERGAIKVDDYCQTSVPGVFAVGDV 292
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
2-274 |
1.07e-10 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 62.10 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQG-APGGQMNNTSDI----------------EN--YPGYDL---ISGPEL 59
Cdd:PRK05249 6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYrNVGGGCTHTGTIpskalreavlrligfnQNplYSSYRVklrITFADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 60 SMKMHE-----------PLEKFGVENLYGIVTAVEDHGnfKKVLTDDNSYET---KTVIIATGAK-HRP--LAVAGEETY 122
Cdd:PRK05249 86 LARADHvinkqvevrrgQYERNRVDLIQGRARFVDPHT--VEVECPDGEVETltaDKIVIATGSRpYRPpdVDFDHPRIY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 123 NSRGV---SYCAvcdgaffrgQDLLVVGGGDSAVEEAlflTRFAN---KVTIVHRRDELraqkvL----QE------RAF 186
Cdd:PRK05249 164 DSDSIlslDHLP---------RSLIIYGAGVIGCEYA---SIFAAlgvKVTLINTRDRL-----LsfldDEisdalsYHL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 187 ANDKVDFIWNSVVKEIKGNDLKVTnVDIEN---VKTGQVnNYAFGGvfiyvgldpvSSMVKELDI------TDEAGWIPT 257
Cdd:PRK05249 227 RDSGVTIRHNEEVEKVEGGDDGVI-VHLKSgkkIKADCL-LYANGR----------TGNTDGLNLenagleADSRGQLKV 294
|
330
....*....|....*..
gi 518635133 258 DDHMKTKAAGVFAIGDV 274
Cdd:PRK05249 295 NENYQTAVPHIYAVGDV 311
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
6-302 |
1.49e-10 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 61.80 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIE-QGAPGGQMNNTSdiENYPGYDLISGPeLSMKMHEplekfgVEN-------LYG 77
Cdd:COG1148 145 VIGGGIAGMTAALELAEQGYEVYLVEkEPELGGRAAQLH--KTFPGLDCPQCI-LEPLIAE------VEAnpnitvyTGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 78 IVTAVEDH-GNFK-KVLTDDNSYETKTV---IIATGAKH-RP----------------------LAVAGEETYNSRG--- 126
Cdd:COG1148 216 EVEEVSGYvGNFTvTIKKGPREEIEIEVgaiVLATGFKPyDPtklgeygygkypnvitnlelerLLAAGKILRPSDGkep 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 127 -----------------VSYC-AVCDGAffrgqdllvvgggdsAVEEALFLtRFAN---KVTIVHRrdELRAQKVLQE-- 183
Cdd:COG1148 296 ksvafiqcvgsrdeengLPYCsRVCCMY---------------ALKQALYL-KEKNpdaDVYIFYR--DIRTYGKYEEfy 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 184 RAFANDKVDFIWNSV--VKEIKGNDLKVTnvdIENVKTGQVNNYAFGGVFIYVGLDPVSSMVKELDI----TDEAGWIpT 257
Cdd:COG1148 358 RRAREDGVRFIRGRVaeIEEDEGGKLVVT---VEDTLLGEPVEIEADLVVLATGMVPSEDNEELAKLlklpLDQDGFF-L 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 518635133 258 DDHMK-----TKAAGVFAIGDVRQ-KDlrqITTAVGDGAVAAQEAYQYIVN 302
Cdd:COG1148 434 EAHPKlrpveTATDGIFLAGAAHGpKD---IPESIAQATAAAARAIQLLSK 481
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-172 |
1.97e-10 |
|
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: 61.03 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGA-PGG--QMNN----TSDIEN----YPGYDLISGPELSMKMHEPL-- 67
Cdd:COG2072 6 HVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADdVGGtwRDNRypglRLDTPShlysLPFFPNWSDDPDFPTGDEILay 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 68 -----EKFGVEN--LYGI-VTAV---EDHGNFkKVLTDD-NSYETKTVIIATGAKHRPL--AVAGEETYnsRGVSY--CA 131
Cdd:COG2072 86 leayaDKFGLRRpiRFGTeVTSArwdEADGRW-TVTTDDgETLTARFVVVATGPLSRPKipDIPGLEDF--AGEQLhsAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518635133 132 VCDGAFFRGQDLLVVGGGDSAVEEALFLTRFANKVTIVHRR 172
Cdd:COG2072 163 WRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
2-100 |
8.82e-10 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 59.13 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQG---------APGGQMNNTSDIENYPgyDLISG-PELSMKMHEPLEKFG 71
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGkklgrkiliSGGGRCNVTNLSEEPD--NFLSRyPGNPKFLKSALSRFT 78
|
90 100 110
....*....|....*....|....*....|....*
gi 518635133 72 VENL------YGIVTAVEDHGnfkKVLTDDNSYET 100
Cdd:pfam03486 79 PWDFiaffesLGVPLKEEDHG---RLFPDSDKASD 110
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
2-273 |
7.72e-09 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 56.55 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGG-----------------QMNNTSDIENYPGYDLISGPELSMKM- 63
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGtcvnvgcvpkkimfnaaSIHDILENSRHYGFDTQFSFNLPLLVe 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 64 -------------HEPLEKFGVENLYGIVTAV-EDHGNFKKVLTDDNSYE----TKTVIIATG-----------AKHRPL 114
Cdd:PTZ00058 129 rrdkyirrlndiyRQNLKKDNVEYFEGKGSLLsENQVLIKKVSQVDGEADesddDEVTIVSAGvsqlddgqvieGKNILI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 115 AVAGE-ETYNSRGVSYCAVCDGaFFR---GQDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDELRaqkvlqeRAFANDk 190
Cdd:PTZ00058 209 AVGNKpIFPDVKGKEFTISSDD-FFKikeAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL-------RKFDET- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 191 vdfIWNSVVKEIKGNDLKVTN----VDIENVKTGQVNNY-AFGGVFIY-------VGLDPVSSMV--KELDITDEAGWIP 256
Cdd:PTZ00058 280 ---IINELENDMKKNNINIIThanvEEIEKVKEKNLTIYlSDGRKYEHfdyviycVGRSPNTEDLnlKALNIKTPKGYIK 356
|
330
....*....|....*..
gi 518635133 257 TDDHMKTKAAGVFAIGD 273
Cdd:PTZ00058 357 VDDNQRTSVKHIYAVGD 373
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-37 |
1.07e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 56.01 E-value: 1.07e-08
10 20 30
....*....|....*....|....*....|....*...
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGA-PGG 37
Cdd:COG1233 3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDtPGG 40
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
6-300 |
1.84e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 55.00 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIE-QGAPGGQMnntsdIENYPGYDL-ISGPELSMKmhePLEKFGVE-----NLYGI 78
Cdd:PRK12770 23 IIGAGPAGLAAAGYLACLGYEVHVYDkLPEPGGLM-----LFGIPEFRIpIERVREGVK---ELEEAGVVfhtrtKVCCG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 79 VTAVEDHG--------NFKKVLTDdnsYETktVIIATGA-KHRPLAVAGEET----------YNSRGVSYC-----AVCD 134
Cdd:PRK12770 95 EPLHEEEGdefverivSLEELVKK---YDA--VLIATGTwKSRKLGIPGEDLpgvysaleylFRIRAAKLGylpweKVPP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 135 gafFRGQDLLVVGGGDSAV---EEALFLTrfANKVTIVHRR--DELRAQKV----LQERAfandkVDFIWNSVVKEIKGN 205
Cdd:PRK12770 170 ---VEGKKVVVVGAGLTAVdaaLEAVLLG--AEKVYLAYRRtiNEAPAGKYeierLIARG-----VEFLELVTPVRIIGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 206 DlKVTNVDIENVK------TGQVNNYAFGG---------VFIYVGLDPVSSMVKE-LDI-TDEAGWIPTDDHMKTKAAGV 268
Cdd:PRK12770 240 G-RVEGVELAKMRlgepdeSGRPRPVPIPGsefvleadtVVFAIGEIPTPPFAKEcLGIeLNRKGEIVVDEKHMTSREGV 318
|
330 340 350
....*....|....*....|....*....|..
gi 518635133 269 FAIGDVRQKDlRQITTAVGDGAVAAQEAYQYI 300
Cdd:PRK12770 319 FAAGDVVTGP-SKIGKAIKSGLRAAQSIHEWL 349
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
1-35 |
3.48e-08 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 54.35 E-value: 3.48e-08
10 20 30
....*....|....*....|....*....|....*
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAP 35
Cdd:COG2509 30 KYDVVIVGAGPAGLFAALELAEAGLKPLVLERGKD 64
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
6-300 |
6.17e-08 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 53.98 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIEQ-GAPGGQMnnTSDIENYPGYDLISGPELsmkmhEPLEKFGVENLYGIVTAved 84
Cdd:PRK12778 436 VIGSGPAGLSFAGDLAKRGYDVTVFEAlHEIGGVL--KYGIPEFRLPKKIVDVEI-----ENLKKLGVKFETDVIVG--- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 85 hgnfKKVLTDDNSYET-KTVIIATGAK-HRPLAVAGEetyNSRGV--------------SYCAVCDGAFFRGQDLLVVGG 148
Cdd:PRK12778 506 ----KTITIEELEEEGfKGIFIASGAGlPNFMNIPGE---NSNGVmssneyltrvnlmdAASPDSDTPIKFGKKVAVVGG 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 149 GDSAVEEALFLTRF-ANKVTIVHRRDELRAQKVLQERAFANDK-VDFIWNSVVKEIKGN-DLKVTNVDIENVKTGQVNN- 224
Cdd:PRK12778 579 GNTAMDSARTAKRLgAERVTIVYRRSEEEMPARLEEVKHAKEEgIEFLTLHNPIEYLADeKGWVKQVVLQKMELGEPDAs 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 225 -----YAFGG---------VFIYVGLDP---VSSMVKELDItDEAGWIPTDDHMKTKAAGVFAIGDVrqkdLRQITT--- 284
Cdd:PRK12778 659 grrrpVAIPGstftvdvdlVIVSVGVSPnplVPSSIPGLEL-NRKGTIVVDEEMQSSIPGIYAGGDI----VRGGATvil 733
|
330
....*....|....*.
gi 518635133 285 AVGDGAVAAQEAYQYI 300
Cdd:PRK12778 734 AMGDGKRAAAAIDEYL 749
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-37 |
7.40e-08 |
|
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: 53.30 E-value: 7.40e-08
10 20 30
....*....|....*....|....*....|....*..
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGG 37
Cdd:COG1053 3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
1-37 |
1.05e-07 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 52.60 E-value: 1.05e-07
10 20 30
....*....|....*....|....*....|....*..
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGG 37
Cdd:COG0665 2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
5-108 |
1.82e-07 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 51.97 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 5 IIIGSGPAGMTAALYAARSNLKVALIEQG---------APGGQMN--NTSDIE----NYPG--------------YDLI- 54
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNpkvgrkiliSGGGRCNftNSEPLPeflnYYGGnphflksalsrftpEDLIa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 55 -------------SG---PElSMK--------MHEpLEKFGVENLYGI-VTAVEDHGNFKKVLTDDN-SYETKTVIIATG 108
Cdd:COG2081 81 ffeglgietkeesSGrvfPD-SSKasdilralLAE-LREAGVEIRLRTrVTGIEKEDGGFGVETPDGeTVRADAVVLATG 158
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
3-86 |
2.36e-07 |
|
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: 51.52 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 3 DTIIIGSGPAGMTAALYAARSNLKVALIEQGAP---------GG-------QMNNTSDIENYPGYDLISGPELSmkmHEP 66
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPfggatawssGGidalgnpPQGGIDSPELHPTDTLKGLDELA---DHP 77
|
90 100
....*....|....*....|
gi 518635133 67 LEKFGVENLYGIVTAVEDHG 86
Cdd:pfam00890 78 YVEAFVEAAPEAVDWLEALG 97
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
2-274 |
1.01e-06 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 49.63 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAP--GGQMNNTSDIenyPGYDLISGPE------LSMKMHEPLEKF--- 70
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAmyGGTCINIGCI---PTKTLVHDAQqhtdfvRAIQRKNEVVNFlrn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 71 -GVENLYGI--VTAVEDHGNF-----KKVLTDDNSYETK--TVIIATGAKHRPLAVAGEET----YNSRGVSYCAVcdga 136
Cdd:PRK08010 81 kNFHNLADMpnIDVIDGQAEFinnhsLRVHRPEGNLEIHgeKIFINTGAQTVVPPIPGITTtpgvYDSTGLLNLKE---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 137 ffRGQDLLVVGGGDSAVEEALFLTRFANKVTIVH-------RRDELRAQ---KVLQERAfandkVDFIWNSVVKEIKGND 206
Cdd:PRK08010 157 --LPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslflpREDRDIADniaTILRDQG-----VDIILNAHVERISHHE 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518635133 207 LKVtNVDIENVKtgqvnnYAFGGVFIYVGLDPVSSMVKELDI---TDEAGWIPTDDHMKTKAAGVFAIGDV 274
Cdd:PRK08010 230 NQV-QVHSEHAQ------LAVDALLIASGRQPATASLHPENAgiaVNERGAIVVDKYLHTTADNIWAMGDV 293
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
5-113 |
1.21e-06 |
|
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: 49.04 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 5 IIIGSGPAGMTAALYAARSNLKVALIEQGApggQMNNTSDienypgydlisgPELSMKMHEPLEKFGVENLYGI-VTAVE 83
Cdd:COG0446 128 VVIGGGPIGLELAEALRKRGLKVTLVERAP---RLLGVLD------------PEMAALLEEELREHGVELRLGEtVVAID 192
|
90 100 110
....*....|....*....|....*....|
gi 518635133 84 DHGNFKKVLTDDNSYETKTVIIATGakHRP 113
Cdd:COG0446 193 GDDKVAVTLTDGEEIPADLVVVAPG--VRP 220
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
1-33 |
1.22e-06 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 49.46 E-value: 1.22e-06
10 20 30
....*....|....*....|....*....|...
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQG 33
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKG 34
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
2-37 |
1.29e-06 |
|
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: 48.85 E-value: 1.29e-06
10 20 30
....*....|....*....|....*....|....*.
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGG 37
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
3-39 |
1.82e-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: 48.76 E-value: 1.82e-06
10 20 30
....*....|....*....|....*....|....*...
gi 518635133 3 DTIIIGSGPAGMTAALYAARSNLKVALIEQ-GAPGGQM 39
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERrGFLGGML 38
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
2-33 |
2.21e-06 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 48.64 E-value: 2.21e-06
10 20 30
....*....|....*....|....*....|..
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQG 33
Cdd:COG3075 3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAG 34
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
2-31 |
4.20e-06 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 47.81 E-value: 4.20e-06
10 20 30
....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIE 31
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVE 46
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
6-39 |
5.72e-06 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 43.29 E-value: 5.72e-06
10 20 30
....*....|....*....|....*....|....*
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIEQGA-PGGQM 39
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDrLGGNA 35
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
91-274 |
6.67e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 47.23 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 91 VLTDDNSYETKTVIIATGAKHRPLAVA---GEETYNSRGVSYCAVCDGAFFRGQDLLVVGGGDSAVEEALFLTRFANKVT 167
Cdd:PRK09754 92 VLTNGESWHWDQLFIATGAAARPLPLLdalGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 168 IVHRRDELRA-------QKVLQERAFANDKVDFIWNSVVKEIKGNDLKVTnvdienVKTGQVnnyAFGGVFIY-VGLDPV 239
Cdd:PRK09754 172 VIELAATVMGrnapppvQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELT------LQSGET---LQADVVIYgIGISAN 242
|
170 180 190
....*....|....*....|....*....|....*
gi 518635133 240 SSMVKELDItDEAGWIPTDDHMKTKAAGVFAIGDV 274
Cdd:PRK09754 243 DQLAREANL-DTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
6-299 |
7.29e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 47.08 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIEQgapggqmnntsdienypgYDLISG------PElsMKMH--------EPLEKFG 71
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVFER------------------ADRIGGllrygiPD--FKLEkevidrriELMEAEG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 72 VENLYGI-----VTAVEDHGNFkkvltdDnsyetkTVIIATGA-KHRPLAVAGEEtynSRGVsYCAV------------- 132
Cdd:PRK12810 208 IEFRTNVevgkdITAEELLAEY------D------AVFLGTGAyKPRDLGIPGRD---LDGV-HFAMdfliqntrrvlgd 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 133 CDGAFFR--GQDLLVVGGGDSAVEEAlfltRFANK--VTIVHRRDE-----LRAQKVLQERAFANDK---------VDFI 194
Cdd:PRK12810 272 ETEPFISakGKHVVVIGGGDTGMDCV----GTAIRqgAKSVTQRDImpmppSRRNKNNPWPYWPMKLevsnaheegVERE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 195 WNSVVKEIKGNDLKVTNVDIENVKTGQVNNYAFGG---------VFIYVGLD-PVSSMVKELDI-TDEAGWI-PTDDHMK 262
Cdd:PRK12810 348 FNVQTKEFEGENGKVTGVKVVRTELGEGDFEPVEGsefvlpadlVLLAMGFTgPEAGLLAQFGVeLDERGRVaAPDNAYQ 427
|
330 340 350
....*....|....*....|....*....|....*...
gi 518635133 263 TKAAGVFAIGD-VRQKDLrqITTAVGDGAVAAQEAYQY 299
Cdd:PRK12810 428 TSNPKVFAAGDmRRGQSL--VVWAIAEGRQAARAIDAY 463
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
2-34 |
1.12e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 46.57 E-value: 1.12e-05
10 20 30
....*....|....*....|....*....|...
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGA 34
Cdd:PRK07843 8 YDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAP 40
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
1-274 |
1.61e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 45.97 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAP---------GGQMNNTS-------------------DIENYpGYD 52
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPstqgtkwglGGTCVNVGcvpkklmhyaanigsifhhDSQMY-GWK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 53 LISGPE--------------LSMKMHEPLEKFGVENLYGIVTAVEDHGNFKKVLTDDNSYETKTVIIATGAK-HRPLAVA 117
Cdd:PTZ00052 84 TSSSFNwgklvttvqnhirsLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQEETITAKYILIATGGRpSIPEDVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 118 GeetynsrGVSYCAVCDGAFFRGQD---LLVVGGGDSAVEEALFLTRFANKVTIVHRRDELRA---QKVLQERAFANDKV 191
Cdd:PTZ00052 164 G-------AKEYSITSDDIFSLSKDpgkTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGfdrQCSEKVVEYMKEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 192 DFIWNSVVKeikgndLKVTNVDiENVKTGQVNNYA--FGGVFIYVGLDPVSSMVK----ELDITDEAGWIPTDDhmKTKA 265
Cdd:PTZ00052 237 TLFLEGVVP------INIEKMD-DKIKVLFSDGTTelFDTVLYATGRKPDIKGLNlnaiGVHVNKSNKIIAPND--CTNI 307
|
....*....
gi 518635133 266 AGVFAIGDV 274
Cdd:PTZ00052 308 PNIFAVGDV 316
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
1-37 |
1.89e-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: 1.89e-05
10 20 30
....*....|....*....|....*....|....*...
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGA-PGG 37
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDrVGG 38
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-35 |
2.32e-05 |
|
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: 45.31 E-value: 2.32e-05
10 20 30
....*....|....*....|....*....|....*
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAP 35
Cdd:COG0654 3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAPP 37
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
89-273 |
2.70e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 45.29 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 89 KKVLTDDNSYETKTVIIATGAKHRPLAVAGEE---TYNSrgVSYCAVCDGAFFRGQDLLVVGGGDSAVEEALFLTRFANK 165
Cdd:PRK04965 89 QVVKSQGNQWQYDKLVLATGASAFVPPIPGRElmlTLNS--QQEYRAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 166 VTIVHRRDEL-----------RAQKVLQERAfandkVDFIWNSVVKEIKGND--LKVTNVDienvktGQVnnYAFGGVFI 232
Cdd:PRK04965 167 VTLVDNAASLlaslmppevssRLQHRLTEMG-----VHLLLKSQLQGLEKTDsgIRATLDS------GRS--IEVDAVIA 233
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518635133 233 YVGLDPVSSMVKELDITDEAGwIPTDDHMKTKAAGVFAIGD 273
Cdd:PRK04965 234 AAGLRPNTALARRAGLAVNRG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
141-282 |
3.53e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 44.77 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 141 QDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDELRA-------QKVLQEraFANDKVDFIWNSVVKEIKGNDLkvtnvd 213
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKlmdadmnQPILDE--LDKREIPYRLNEEIDAINGNEV------ 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 214 ieNVKTGQVNNYAFggVFIYVGLDPVSSMVKELDIT-DEAGWIPTDDHMKTKAAGVFAIGDVRQKDLRQI 282
Cdd:PRK13512 221 --TFKSGKVEHYDM--IIEGVGTHPNSKFIESSNIKlDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
3-38 |
3.77e-05 |
|
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: 44.70 E-value: 3.77e-05
10 20 30
....*....|....*....|....*....|....*.
gi 518635133 3 DTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQ 38
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
3-39 |
4.22e-05 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 44.00 E-value: 4.22e-05
10 20 30
....*....|....*....|....*....|....*....
gi 518635133 3 DTIIIGSGPAGMTAALYAARS-NLKVALIEQG-APGGQM 39
Cdd:pfam01946 19 DVVIVGAGSSGLTAAYYLAKNrGLKVAIIERSvSPGGGA 57
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
141-274 |
4.67e-05 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 44.56 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 141 QDLLVVGGGDSAVEEALFLTRFANKVTIVHRRDE-LRAQKVLQERAF---ANDKVDFIWNSVVKEIKGNDLKVT------ 210
Cdd:PRK07846 167 ESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRlLRHLDDDISERFtelASKRWDVRLGRNVVGVSQDGSGVTlrlddg 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518635133 211 ---NVDIENVKTGQVNNyafGGVfiyvgLDPVSSMVKeldiTDEAGWIPTDDHMKTKAAGVFAIGDV 274
Cdd:PRK07846 247 stvEADVLLVATGRVPN---GDL-----LDAAAAGVD----VDEDGRVVVDEYQRTSAEGVFALGDV 301
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
2-33 |
9.77e-05 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 43.47 E-value: 9.77e-05
10 20 30
....*....|....*....|....*....|..
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQG 33
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAG 32
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
3-125 |
9.87e-05 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 43.31 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 3 DTIIIGSGPAGMTAALYAARSNLKVALI--------------------------EQGAPGGQMNNTSDiENYPGYDLIS- 55
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLIthntdtiaelscnpsiggiakghlvrEIDALGGLMGKAAD-KTGIQFRMLNt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 56 --GP------------ELSMKMHEPLEKFgvENLY---GIVTAVEDHGN-FKKVLTDDNS-YETKTVIIATGAKHRPLAV 116
Cdd:pfam01134 80 skGPavralraqvdrdLYSKEMTETLENH--PNLTliqGEVTDLIPENGkVKGVVTEDGEeYKAKAVVLATGTFLNGKIH 157
|
....*....
gi 518635133 117 AGEETYNSR 125
Cdd:pfam01134 158 IGLKCYPAG 166
|
|
| NadB |
COG0029 |
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ... |
1-30 |
1.03e-04 |
|
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439800 [Multi-domain] Cd Length: 521 Bit Score: 43.56 E-value: 1.03e-04
10 20 30
....*....|....*....|....*....|
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARsNLKVALI 30
Cdd:COG0029 4 KTDVLVIGSGIAGLSAALKLAE-RGRVTLL 32
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
2-32 |
1.91e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 42.62 E-value: 1.91e-04
10 20 30
....*....|....*....|....*....|.
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQ 32
Cdd:PRK09126 4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| PRK07608 |
PRK07608 |
UbiH/UbiF family hydroxylase; |
2-35 |
2.15e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181057 [Multi-domain] Cd Length: 388 Bit Score: 42.25 E-value: 2.15e-04
10 20 30
....*....|....*....|....*....|....
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAP 35
Cdd:PRK07608 6 FDVVVVGGGLVGASLALALAQSGLRVALLAPRAP 39
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
5-274 |
3.49e-04 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 41.77 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 5 IIIGSGPAGMTAALYAARSNLKVALIEQGAPGG------------------QMNNTSDIENYpGYDLISGPEL------- 59
Cdd:PRK07845 5 VIIGGGPGGYEAALVAAQLGADVTVIERDGLGGaavltdcvpsktliataeVRTELRRAAEL-GIRFIDDGEArvdlpav 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 60 -----------SMKMHEPLEKFGVENLYGI--VTAVEDHGNFKKVLTDDNSYET---KTVIIATGAKHRPLAVA---GEE 120
Cdd:PRK07845 84 narvkalaaaqSADIRARLEREGVRVIAGRgrLIDPGLGPHRVKVTTADGGEETldaDVVLIATGASPRILPTAepdGER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 121 TYNSRGVsYcavcdgaffrgqD-------LLVVGGGDSAVEEALFLTRFANKVTIVHRRDEL------RAQKVLqERAFA 187
Cdd:PRK07845 164 ILTWRQL-Y------------DldelpehLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVlpgedaDAAEVL-EEVFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 188 NDKVDFIWNSVVKEIK--GNDLKVTNVDIENVK-------TGQVNNYAfggvfiYVGLDPVSsmVKeldiTDEAGWIPTD 258
Cdd:PRK07845 230 RRGMTVLKRSRAESVErtGDGVVVTLTDGRTVEgshalmaVGSVPNTA------GLGLEEAG--VE----LTPSGHITVD 297
|
330
....*....|....*.
gi 518635133 259 DHMKTKAAGVFAIGDV 274
Cdd:PRK07845 298 RVSRTSVPGIYAAGDC 313
|
|
| solA |
PRK11259 |
N-methyl-L-tryptophan oxidase; |
2-39 |
3.61e-04 |
|
N-methyl-L-tryptophan oxidase;
Pssm-ID: 236887 [Multi-domain] Cd Length: 376 Bit Score: 41.75 E-value: 3.61e-04
10 20 30
....*....|....*....|....*....|....*...
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQM 39
Cdd:PRK11259 4 YDVIVIGLGSMGSAAGYYLARRGLRVLGLDRFMPPHQQ 41
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
2-32 |
4.66e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 41.63 E-value: 4.66e-04
10 20 30
....*....|....*....|....*....|.
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQ 32
Cdd:PRK06134 13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEK 43
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
6-37 |
5.06e-04 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 41.68 E-value: 5.06e-04
10 20 30
....*....|....*....|....*....|..
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIEQGAPGG 37
Cdd:PRK13748 103 VIGSGGAAMAAALKAVEQGARVTLIERGTIGG 134
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
1-34 |
5.49e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 41.33 E-value: 5.49e-04
10 20 30
....*....|....*....|....*....|....
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGA 34
Cdd:PRK12835 11 EVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSA 44
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
99-290 |
5.58e-04 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 41.11 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 99 ETKTVIIATGAKHRPLAVAGEEtynsrgvsYCAVCDGAFFRGQD---LLVVGGGDSAVEEALFLTRF---ANKVTIVHRR 172
Cdd:TIGR01423 151 QAEHILLATGSWPQMLGIPGIE--------HCISSNEAFYLDEPprrVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518635133 173 D--------ELRAQKVLQERAfanDKVDFIWNSVVKEIKGNDLKVTNVDIENVKTGQVNNyafggVFIYVGLDPVSSMVK 244
Cdd:TIGR01423 223 NmilrgfdsTLRKELTKQLRA---NGINIMTNENPAKVTLNADGSKHVTFESGKTLDVDV-----VMMAIGRVPRTQTLQ 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518635133 245 ----ELDITDEAGwIPTDDHMKTKAAGVFAIGDVRQKdLRQITTAVGDGA 290
Cdd:TIGR01423 295 ldkvGVELTKKGA-IQVDEFSRTNVPNIYAIGDVTDR-VMLTPVAINEGA 342
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-42 |
9.20e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 40.27 E-value: 9.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNT 42
Cdd:PRK07494 7 HTDIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTT 48
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
3-32 |
9.25e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 40.64 E-value: 9.25e-04
10 20 30
....*....|....*....|....*....|
gi 518635133 3 DTIIIGSGPAGMTAALYAARSNLKVALIEQ 32
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEA 35
|
|
| PRK10015 |
PRK10015 |
oxidoreductase; Provisional |
2-42 |
2.26e-03 |
|
oxidoreductase; Provisional
Pssm-ID: 182194 [Multi-domain] Cd Length: 429 Bit Score: 39.19 E-value: 2.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNT 42
Cdd:PRK10015 6 FDAIVVGAGVAGSVAALVMARAGLDVLVIERGDSAGCKNMT 46
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
2-32 |
2.47e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 39.35 E-value: 2.47e-03
10 20 30
....*....|....*....|....*....|.
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQ 32
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEK 37
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
10-73 |
2.60e-03 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 38.80 E-value: 2.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518635133 10 GPAGMTAALYAARSNLKVALIEQGApggqmnntsdienYPGYDLISGpELSMKMHEPLEKFGVE 73
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGS-------------FPGDKICGG-GLLPRALEELEPLGLD 51
|
|
| PRK05732 |
PRK05732 |
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated |
1-52 |
2.87e-03 |
|
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
Pssm-ID: 235584 [Multi-domain] Cd Length: 395 Bit Score: 39.07 E-value: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 518635133 1 MYDTIIIGSGPAGMTAAL---YAARSNLKVALIEQGAPGGQMnntsdienYPGYD 52
Cdd:PRK05732 3 RMDVIIVGGGMAGATLALalsRLSHGGLPVALIEAFAPESDA--------HPGFD 49
|
|
| PRK10157 |
PRK10157 |
putative oxidoreductase FixC; Provisional |
1-42 |
2.96e-03 |
|
putative oxidoreductase FixC; Provisional
Pssm-ID: 182273 [Multi-domain] Cd Length: 428 Bit Score: 39.12 E-value: 2.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNT 42
Cdd:PRK10157 5 IFDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVT 46
|
|
| PRK09077 |
PRK09077 |
L-aspartate oxidase; Provisional |
2-34 |
3.20e-03 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236374 [Multi-domain] Cd Length: 536 Bit Score: 39.13 E-value: 3.20e-03
10 20 30
....*....|....*....|....*....|...
gi 518635133 2 YDTIIIGSGPAGMTAALYAArSNLKVALIEQGA 34
Cdd:PRK09077 9 CDVLIIGSGAAGLSLALRLA-EHRRVAVLSKGP 40
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
2-32 |
4.14e-03 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 38.66 E-value: 4.14e-03
10 20 30
....*....|....*....|....*....|.
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQ 32
Cdd:PRK06481 62 YDIVIVGAGGAGMSAAIEAKDAGMNPVILEK 92
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
2-38 |
4.65e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 38.34 E-value: 4.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIEQGAP---GGQ 38
Cdd:PRK12834 5 ADVIVVGAGLAGLVAAAELADAGKRVLLLDQENEanlGGQ 44
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
6-49 |
4.67e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 38.33 E-value: 4.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIEQGAPGGQMNNTSDIENYP 49
Cdd:PRK07233 4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLP 47
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
6-32 |
4.80e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 38.30 E-value: 4.80e-03
10 20
....*....|....*....|....*..
gi 518635133 6 IIGSGPAGMTAALYAARSNLKVALIEQ 32
Cdd:PRK06185 11 IVGGGPAGMMLGLLLARAGVDVTVLEK 37
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
1-35 |
5.58e-03 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 37.93 E-value: 5.58e-03
10 20 30
....*....|....*....|....*....|....*
gi 518635133 1 MYDTIIIGSGPAGMTAALYAARSNLKVALIEQgAP 35
Cdd:PRK08274 4 MVDVLVIGGGNAALCAALAAREAGASVLLLEA-AP 37
|
|
| PRK07364 |
PRK07364 |
FAD-dependent hydroxylase; |
2-31 |
7.12e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236001 [Multi-domain] Cd Length: 415 Bit Score: 37.69 E-value: 7.12e-03
10 20 30
....*....|....*....|....*....|
gi 518635133 2 YDTIIIGSGPAGMTAALYAARSNLKVALIE 31
Cdd:PRK07364 19 YDVAIVGGGIVGLTLAAALKDSGLRIALIE 48
|
|
| |
