|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
1-441 |
0e+00 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 902.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQRKNEVVNFLRN 80
Cdd:PRK08010 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQRKNEVVNFLRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 81 KNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEANLEIHGEKIFINTGAQTVVPPIPGITTTPGVYDSTGLLNLKELPGH 160
Cdd:PRK08010 81 KNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEIHGEKIFINTGAQTVVPPIPGITTTPGVYDSTGLLNLKELPGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 161 LGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQ 240
Cdd:PRK08010 161 LGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 241 LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGRR 320
Cdd:PRK08010 241 LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 321 STDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSH 400
Cdd:PRK08010 321 STDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSH 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446969037 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSLVK 441
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSLVK 441
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
1-441 |
0e+00 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 861.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQRKNEVVNFLRN 80
Cdd:NF040477 1 MNHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMYGGTCINIGCIPTKTLVHDAEQHQDFSTAMQRKSSVVGFLRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 81 KNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEANLEIHGEKIFINTGAQTVVPPIPGITTTPGVYDSTGLLNLKELPGH 160
Cdd:NF040477 81 KNYHNLADLDNVDVINGRAEFIDNHTLRVFQADGEQELRGEKIFINTGAQSVLPPIPGLTTTPGVYDSTGLLNLTQLPAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 161 LGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQ 240
Cdd:NF040477 161 LGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSHEGEVQLETAEGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 241 LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGRR 320
Cdd:NF040477 241 LTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQFTYISLDDFRIVRDSLLGEGKR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 321 STDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSH 400
Cdd:NF040477 321 STDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVLKAVVDNKTQRILGVSLLCVDSH 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446969037 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSLVK 441
Cdd:NF040477 401 EMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDLFALIK 441
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
1-439 |
6.71e-179 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 506.59 E-value: 6.71e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQRKNEVVNFLRN 80
Cdd:PRK07251 1 MLTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMYGGTCINIGCIPTKTLLVAAEKNLSFEQVMATKNTVTSRLRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 81 KNFHNLADmPNIDVIDGQAEFINNHSLRVHRPEANLEIHGEKIFINTGAQTVVPPIPGITTTPGVYDSTGLLNLKELPGH 160
Cdd:PRK07251 81 KNYAMLAG-SGVDLYDAEAHFVSNKVIEVQAGDEKIELTAETIVINTGAVSNVLPIPGLADSKHVYDSTGIQSLETLPER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 161 LGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQ 240
Cdd:PRK07251 160 LGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVVTEDET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 241 LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGRR 320
Cdd:PRK07251 240 YRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGDGSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 321 STDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSH 400
Cdd:PRK07251 320 TLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKVVVNTETKEILGATLFGEGSQ 399
|
410 420 430
....*....|....*....|....*....|....*....
gi 446969037 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSL 439
Cdd:PRK07251 400 EIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLFNI 438
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-437 |
3.91e-154 |
|
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: 444.53 E-value: 3.91e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSnaMYGGTCINIGCIPTKTLVHDAQQ-----------------HTD 63
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKG--RLGGTCLNVGCIPSKALLHAAEVahearhaaefgisagapSVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 64 FVRAIQRKNEVVNFLRNKNfHNLADMPNIDVIDGQAEFINNHSLRVHRPEanlEIHGEKIFINTGAQTVVPPIPGITTtP 143
Cdd:COG1249 79 WAALMARKDKVVDRLRGGV-EELLKKNGVDVIRGRARFVDPHTVEVTGGE---TLTADHIVIATGSRPRVPPIPGLDE-V 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 144 GVYDSTGLLNLKELP-----------GhlgilgggyigVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQ 212
Cdd:COG1249 154 RVLTSDEALELEELPkslvvigggyiG-----------LEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 213 GVDIILNAHVERISHHENQVQVHSEH----AQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIW 288
Cdd:COG1249 223 GIDILTGAKVTSVEKTGDGVTVTLEDgggeEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 289 AMGDVTGGLQFTYISLDDYRIVRDELLGEGRRSTDDRkNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRA 368
Cdd:COG1249 303 AIGDVTGGPQLAHVASAEGRVAAENILGKKPRPVDYR-AIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446969037 369 RVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLF 437
Cdd:COG1249 382 LALGETEGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-437 |
2.29e-143 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 417.30 E-value: 2.29e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEqsNAMYGGTCINIGCIPTKTLV------HDAQQHT------------ 62
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIE--RGLLGGTCVNTGCVPTKTLIasaraaHLARRAAeygvsvggpvsv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 63 DFVRAIQRKNEVVNFLRNKNFHNLADMPNIDVIDGQAEFINNHSLRVhrpeANLEIHGEKIFINTGAQTVVPPIPGITTT 142
Cdd:PRK06370 81 DFKAVMARKRRIRARSRHGSEQWLRGLEGVDVFRGHARFESPNTVRV----GGETLRAKRIFINTGARAAIPPIPGLDEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 143 PgVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHV 222
Cdd:PRK06370 157 G-YLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAEC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 223 ERISHHENQVQVHSEHA----QLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQ 298
Cdd:PRK06370 236 IRVERDGDGIAVGLDCNggapEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 299 FTYISLDDYRIVRDELLGEGRRSTDDRkNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVL 378
Cdd:PRK06370 316 FTHTAYNDARIVAANLLDGGRRKVSDR-IVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFM 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446969037 379 KAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLF 437
Cdd:PRK06370 395 KVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLA 453
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-433 |
3.18e-100 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 306.72 E-value: 3.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQ-----QHT------------D 63
Cdd:PRK06292 1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGP--LGGTCLNVGCIPSKALIAAAEafheaKHAeefgihadgpkiD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 64 FVRAIQRKNEVVNFLRNKNFHNLADMPNIDVIDGQAEFINNHSLRVHrpeaNLEIHGEKIFINTGAQtvVPPIPGIT--T 141
Cdd:PRK06292 79 FKKVMARVRRERDRFVGGVVEGLEKKPKIDKIKGTARFVDPNTVEVN----GERIEAKNIVIATGSR--VPPIPGVWliL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 142 TPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQgVDIILNAH 221
Cdd:PRK06292 153 GDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 222 VERISHHENQVQVHSEHA----QLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGL 297
Cdd:PRK06292 232 VTSVEKSGDEKVEELEKGgkteTIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 298 QFTYISLDDYRIVRDELLGeGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGV 377
Cdd:PRK06292 312 PLLHEAADEGRIAAENAAG-DVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446969037 378 LKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:PRK06292 391 VKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGL 446
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
4-433 |
9.20e-97 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 298.18 E-value: 9.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQsnAMYGGTCINIGCIPTKTLV----------------HDAQQHTDFVRA 67
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVER--GPLGGTCVNVGCVPSKMLLraaevahyarkppfggLAATVAVDFGEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 68 IQRKNEVVNFLRNKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEanlEIHGEKIF-INTGAQTVVPPIPGITTTpGVY 146
Cdd:TIGR02053 79 LEGKREVVEELRHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDLGR---EVRGAKRFlIATGARPAIPPIPGLKEA-GYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 147 DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERIS 226
Cdd:TIGR02053 155 TSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 227 HHENQVQVHSE----HAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQFTYI 302
Cdd:TIGR02053 235 VRGGGKIITVEkpggQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 303 SLDDYRIVRDELLGeGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIV 382
Cdd:TIGR02053 315 AAKEGVVAAENALG-GANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLVA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446969037 383 DNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:TIGR02053 394 EPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGL 444
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
4-433 |
2.01e-96 |
|
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: 297.25 E-value: 2.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQQHT-----------------DFVR 66
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEY--LGGTCLNVGCIPTKALLHSAEVYDeikhakdlgievenvsvDWEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 67 AIQRKNEVVNFLRnKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEANLEIHGEKIFINTGAQTVVPPIPGITTTPGVY 146
Cdd:TIGR01350 80 MQKRKNKVVKKLV-GGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETLEAKNIIIATGSRPRSLPGPFDFDGKVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 147 DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERIS 226
Cdd:TIGR01350 159 TSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 227 HHENQVQVH---SEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQFTYIS 303
Cdd:TIGR01350 239 KNDDQVTYEnkgGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 304 LDDYRIVRDELLGEgRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVD 383
Cdd:TIGR01350 319 SHEGIVAAENIAGK-EPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIAD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446969037 384 NKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:TIGR01350 398 KKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAI 447
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
4-433 |
2.74e-85 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 268.55 E-value: 2.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVH---------DAQQ---HTDFVR----A 67
Cdd:PRK06416 5 YDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK--LGGTCLNRGCIPSKALLHaaeradearHSEDfgiKAENVGidfkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 68 IQ-RKNEVVNFLRnKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEANLEIHGEKIFINTGAQTVVppIPGITTTPG-V 145
Cdd:PRK06416 83 VQeWKNGVVNRLT-GGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTYTAKNIILATGSRPRE--LPGIEIDGRvI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 146 YDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERI 225
Cdd:PRK06416 160 WTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 226 SHHENQVQVHSEHA----QLAVDALLIASGRQPATASLHPENAGIAVnERGAIVVDKQLHTTADNIWAMGDVTGGLQFTY 301
Cdd:PRK06416 240 EQTDDGVTVTLEDGgkeeTLEADYVLVAVGRRPNTENLGLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 302 ISLDDYRIVRDELLgeGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAI 381
Cdd:PRK06416 319 KASAEGIIAAEAIA--GNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLI 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446969037 382 VDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:PRK06416 397 FDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEAL 448
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
5-433 |
8.33e-77 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 249.30 E-value: 8.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 5 QAVIIGFGKAGKTLAVTLAKAGWRVALIEQSnaMYGGTCINIGCIPTKTLV---HDAQQHTD--F-------VRAIQRKN 72
Cdd:PRK13748 100 HVAVIGSGGAAMAAALKAVEQGARVTLIERG--TIGGTCVNVGCVPSKIMIraaHIAHLRREspFdggiaatVPTIDRSR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 73 EV------VNFLRNKNFHN-LADMPNIDVIDGQAEFINNHSLRVHRPE-ANLEIHGEKIFINTGAQTVVPPIPGITTTPg 144
Cdd:PRK13748 178 LLaqqqarVDELRHAKYEGiLDGNPAITVLHGEARFKDDQTLIVRLNDgGERVVAFDRCLIATGASPAVPPIPGLKETP- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 145 VYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLpREDRDIADNIATILRDQGVDIILNAHVER 224
Cdd:PRK13748 257 YWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFF-REDPAIGEAVTAAFRAEGIEVLEHTQASQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 225 ISHHENQVQVHSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQFTYISL 304
Cdd:PRK13748 336 VAHVDGEFVLTTGHGELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 305 DDYriVRDELLGEGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDN 384
Cdd:PRK13748 416 AAG--TRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGFIKLVIEE 493
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446969037 385 KTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:PRK13748 494 GSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGL 542
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-432 |
2.15e-76 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 245.45 E-value: 2.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNaMYGGTCINIGCIPTKTLVHDAQQHT-----DFVRAIQRK---- 71
Cdd:PRK05249 3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYR-NVGGGCTHTGTIPSKALREAVLRLIgfnqnPLYSSYRVKlrit 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 72 --------NEVVN---------FLRNKnfhnladmpnIDVIDGQAEFINNHSLRVHRPEANLE-IHGEKIFINTGAQTVV 133
Cdd:PRK05249 82 fadllaraDHVINkqvevrrgqYERNR----------VDLIQGRARFVDPHTVEVECPDGEVEtLTADKIVIATGSRPYR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 134 PP-IPgiTTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQ 212
Cdd:PRK05249 152 PPdVD--FDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 213 GVDIILNAHVERISHHENQVQVHSEH-AQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMG 291
Cdd:PRK05249 230 GVTIRHNEEVEKVEGGDDGVIVHLKSgKKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 292 DVTG--GLQFTyiSLDDYRIVRDELLGE--GRRSTDdrknVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPR 367
Cdd:PRK05249 310 DVIGfpSLASA--SMDQGRIAAQHAVGEatAHLIED----IPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKELAR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446969037 368 ARVMNDTRGVLKAIVDNKTQRILGASllCVDSH--EMINIVKMVMDAGLPYSILRDQIFTHPSMSES 432
Cdd:PRK05249 384 AQIAGDNVGMLKILFHRETLEILGVH--CFGERatEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEA 448
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-433 |
1.96e-70 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 230.20 E-value: 1.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIE-----QSNAMYGGTCINIGCIPTKTLV----------HDAQQH---- 61
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpKGKPALGGTCLNVGCIPSKALLasseefenagHHFADHgihv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 62 ----TDFVRAIQRKNEVVN-------FLRNKNfhnladmpNIDVIDGQAEFINN----HSLRVhRPEANLEIHGEKIFIN 126
Cdd:PRK06327 82 dgvkIDVAKMIARKDKVVKkmtggieGLFKKN--------KITVLKGRGSFVGKtdagYEIKV-TGEDETVITAKHVIIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 127 TGAQTVvpPIPGITT-TPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNI 205
Cdd:PRK06327 153 TGSEPR--HLPGVPFdNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 206 ATILRDQGVDIILNAHVERISHHENQVQV-----HSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQL 280
Cdd:PRK06327 231 AKAFTKQGLDIHLGVKIGEIKTGGKGVSVaytdaDGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 281 HTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEgrRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTL 360
Cdd:PRK06327 311 RTNVPNVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQ--KGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKF 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446969037 361 PVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:PRK06327 389 PFMANGRALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVW 461
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
4-431 |
4.48e-70 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 228.68 E-value: 4.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGkAGKTLaVTLAKAGWRVALIEQsnAMYGGTCINIGCIPTKTLVHDAqqhtDFVRAIQRKNEV-VNF----- 77
Cdd:PRK07846 2 YDLIIIGTG-SGNSI-LDERFADKRIAIVEK--GTFGGTCLNVGCIPTKMFVYAA----DVARTIREAARLgVDAeldgv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 78 ----LRNKNFHNL------------ADMPNIDVIDGQAEFINNHSLRVHRPEanlEIHGEKIFINTGAQTVVPPIPGITT 141
Cdd:PRK07846 74 rwpdIVSRVFGRIdpiaaggeeyrgRDTPNIDVYRGHARFIGPKTLRTGDGE---EITADQVVIAAGSRPVIPPVIADSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 142 TPgVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRdQGVDIILNAH 221
Cdd:PRK07846 151 VR-YHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELAS-KRWDVRLGRN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 222 VERISHHENQVQVHSEHAQ-LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQFT 300
Cdd:PRK07846 229 VVGVSQDGSGVTLRLDDGStVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 301 YISLDDYRIVRDELL-GEGRRSTDDRkNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLK 379
Cdd:PRK07846 309 HVANHEARVVQHNLLhPDDLIASDHR-FVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAMEDTTGFVK 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446969037 380 AIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLP-YSILRDQIFTHPSMSE 431
Cdd:PRK07846 388 LIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDaREMARGQYWIHPALPE 440
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
9-431 |
2.26e-64 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 213.86 E-value: 2.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 9 IGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQ------------------QHTDFVRAIQR 70
Cdd:PRK06116 10 IGGGSGGIASANRAAMYGAKVALIEAKR--LGGTCVNVGCVPKKLMWYGAQiaeafhdyapgygfdvteNKFDWAKLIAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 71 KNEVVNFLrNKNFHNLADMPNIDVIDGQAEFINNHSLRVhrpeANLEIHGEKIFINTGAQTVVPPIPGITTTpgvYDSTG 150
Cdd:PRK06116 88 RDAYIDRL-HGSYRNGLENNGVDLIEGFARFVDAHTVEV----NGERYTADHILIATGGRPSIPDIPGAEYG---ITSDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 151 LLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHEN 230
Cdd:PRK06116 160 FFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 231 -QVQVHSEHAQ-LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGLQFTYISLDDYR 308
Cdd:PRK06116 240 gSLTLTLEDGEtLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 309 IVRDELLGEGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVtlpvaaIPRA--RVM------NDTRGVLKA 380
Cdd:PRK06116 320 RLSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVK------VYRSsfTPMytaltgHRQPCLMKL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446969037 381 IVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
Cdd:PRK06116 394 VVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
4-431 |
1.06e-57 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 196.13 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGkAGKTLaVTLAKAGWRVALIEQsnAMYGGTCINIGCIPTKTLVHDAQ--------------QHTDFVR--A 67
Cdd:TIGR03452 3 YDLIIIGTG-SGNSI-PDPRFADKRIAIVEK--GTFGGTCLNVGCIPTKMFVYAAEvaqsigesarlgidAEIDSVRwpD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 68 IQRKnevVNFLR-------NKNFHNLADMPNIDVIDGQAEFINNHSLRVhrpEANLEIHGEKIFINTGAQTVVPPipgIT 140
Cdd:TIGR03452 79 IVSR---VFGDRidpiaagGEDYRRGDETPNIDVYDGHARFVGPRTLRT---GDGEEITGDQIVIAAGSRPYIPP---AI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 141 TTPGV--YDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQgVDIIL 218
Cdd:TIGR03452 150 ADSGVryHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDISDRFTEIAKKK-WDIRL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 219 NAHVERISHHENQVQVHSEHAQ-LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGGL 297
Cdd:TIGR03452 229 GRNVTAVEQDGDGVTLTLDDGStVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWALGDVSSPY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 298 QFTYISLDDYRIVRDELLGEGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGV 377
Cdd:TIGR03452 309 QLKHVANAEARVVKHNLLHPNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNYGDVAYGWAMEDTTGF 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446969037 378 LKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLP-YSILRDQIFTHPSMSE 431
Cdd:TIGR03452 389 CKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDaREMARKQYWIHPALPE 443
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
4-296 |
9.08e-52 |
|
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: 176.35 E-value: 9.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQsnamyGGTCINIGCIPTKTLVHDAQQHTDFVR---AIQRKNEVVNFLRN 80
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED-----EGTCPYGGCVLSKALLGAAEAPEIASLwadLYKRKEEVVKKLNN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 81 kNFHNLADMPNIDVIDGQAEFINNHSLRVHrpeaNLEIHGEKIFINTGAQTVVPPIPGITTTPG----VYDSTGLLNLKE 156
Cdd:pfam07992 76 -GIEVLLGTEVVSIDPGAKKVVLEELVDGD----GETITYDRLVIATGARPRLPPIPGVELNVGflvrTLDSAEALRLKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 157 LPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVH- 235
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIl 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446969037 236 SEHAQLAVDALLIASGRQPATASLhpENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGG 296
Cdd:pfam07992 231 KDGTEIDADLVVVAIGRRPNTELL--EAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVG 289
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
4-441 |
7.92e-50 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 176.54 E-value: 7.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIE--------QSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQ---RKN 72
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNygwEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 73 EVVNF-----LRNKN---------FHNLADMPNIDVIDGQAEFINNHSLRVHRPEAN-LEIHGEKIFINTGAQTVVPPIP 137
Cdd:PLN02507 106 EKVDFnwkklLQKKTdeilrlngiYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTkLRYTAKHILIATGSRAQRPNIP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 138 G----ITTTPGvydstglLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQG 213
Cdd:PLN02507 186 GkelaITSDEA-------LSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 214 VDIILNAHVERISHHENQVQVHSEHA-QLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGD 292
Cdd:PLN02507 259 INLHPRTNLTQLTKTEGGIKVITDHGeEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 293 VTGGLQFTYISLDDYRIVRDELLGeGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQA-RESGADIQVVTLPVAAIPRARVM 371
Cdd:PLN02507 339 VTNRINLTPVALMEGTCFAKTVFG-GQPTKPDYENVACAVFCIPPLSVVGLSEEEAvEQAKGDILVFTSSFNPMKNTISG 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 372 NDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSLVK 441
Cdd:PLN02507 418 RQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMRSVTR 487
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
4-433 |
1.63e-41 |
|
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: 153.59 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGktlavtlAKAGW--------RVALIEQSN-------AMYGGTCINIGCIPTKTLVHDAQqHTDFVRA- 67
Cdd:TIGR01423 4 FDLVVIGAGSGG-------LEAGWnaatlykkRVAVVDVQThhgppfyAALGGTCVNVGCVPKKLMVTGAQ-YMDTLREs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 68 -------------------IQRKNEVVNFLrNKNFHNL-ADMPNIDVIDGQAEFINNHSLRVHR---PEANLE--IHGEK 122
Cdd:TIGR01423 76 agfgwefdrssvkanwkalIAAKNKAVLDI-NKSYEGMfADTEGLTFFLGWGALEDKNVVLVREsadPKSAVKerLQAEH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 123 IFINTGAQTVVPPIPG----ITTTPGVYdstgllnLKELPGHLGILGGGYIGVEFASMFANF---GSKVTILEAASLFLP 195
Cdd:TIGR01423 155 ILLATGSWPQMLGIPGiehcISSNEAFY-------LDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNMILR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 196 REDRDIADNIATILRDQGVDIILNAHVERISHHENQVQ--VHSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGA 273
Cdd:TIGR01423 228 GFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKhvTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 274 IVVDKQLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGRRSTDDRKnVPYSVFMTPPLSRVGMTEEQARESGA 353
Cdd:TIGR01423 308 IQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTR-VASAVFSIPPIGTCGLVEEDAAKKFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 354 diQVVTLPVAAIPrarVMNDTRG------VLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHP 427
Cdd:TIGR01423 387 --KVAVYESSFTP---LMHNISGskykkfVAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHP 461
|
....*.
gi 446969037 428 SMSESL 433
Cdd:TIGR01423 462 TSAEEL 467
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
4-433 |
3.67e-38 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 145.40 E-value: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIE------QSNAM--YGGTCINIGCIPTKTLVHDAQQHTDF--------VRA 67
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCElpfatiSSDTLggVGGTCVLRGCVPKKLLVYASKYSHEFeesrgfgwKYE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 68 IQRKNEVVNFLRNKN---------FHNLADMPNIDVIDGQAEFINNHSLRVhrpeaNLEIHGEK-IFINTGAQTVVPPIP 137
Cdd:PLN02546 160 TEPKHDWNTLIANKNaelqrltgiYKNILKNAGVTLIEGRGKIVDPHTVDV-----DGKLYTARnILIAVGGRPFIPDIP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 138 GITTtpgVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIi 217
Cdd:PLN02546 235 GIEH---AIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEF- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 218 lnaHVERishhENQVQVHSEHAQLAVDA----------LLIASGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNI 287
Cdd:PLN02546 311 ---HTEE----SPQAIIKSADGSLSLKTnkgtvegfshVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSI 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 288 WAMGDVTGGLQFTYISLDDYRIVRDELLGEGRRSTDDRKnVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPR 367
Cdd:PLN02546 384 WAVGDVTDRINLTPVALMEGGALAKTLFGNEPTKPDYRA-VPSAVFSQPPIGQVGLTEEQAIEEYGDVDVFTANFRPLKA 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446969037 368 ARVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:PLN02546 463 TLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF 528
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
328-433 |
4.94e-35 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 125.74 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 328 VPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVK 407
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*.
gi 446969037 408 MVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEAL 106
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
2-437 |
1.02e-34 |
|
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: 134.98 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 2 NKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAM-------YGGTCINIGCIPTKtLVHDAQ------QHTD----- 63
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTplgtrwgIGGTCVNVGCIPKK-LMHQAAllgqalKDSRnygwk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 64 -----------FVRAIQRKNEVVNF-----LRNKNfhnladmpnIDVIDGQAEFINNHSLRVHRPEANLEIH-GEKIFIN 126
Cdd:TIGR01438 80 veetvkhdwkrLVEAVQNHIGSLNWgyrvaLREKK---------VKYENAYAEFVDKHRIKATNKKGKEKIYsAERFLIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 127 TGAQTVVPPIPG-----ITttpgvydSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeAASLFLPREDRDI 201
Cdd:TIGR01438 151 TGERPRYPGIPGakelcIT-------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 202 ADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAV----DALLIASGRQPATASLHPENAGIAVNER-GAIVV 276
Cdd:TIGR01438 223 ANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIeeeyDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 277 DKQLHTTADNIWAMGDVTGG-LQFTYISLDDYRIVRDELLGeGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARES-GAD 354
Cdd:TIGR01438 303 DEEEQTNVPYIYAVGDILEDkPELTPVAIQAGRLLAQRLFK-GSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKfGEE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 355 -IQVVTLPVAAIPRARVMNDTRG--VLKAIVD-NKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMS 430
Cdd:TIGR01438 382 nVEVFHSYFWPLEWTIPSRDNHNkcYAKLVCNkKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCA 461
|
....*..
gi 446969037 431 ESLNDLF 437
Cdd:TIGR01438 462 EVFTTLS 468
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
7-433 |
2.72e-34 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 133.45 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 7 VIIGFGKAGKTLAVTLAKAGWRVALIEQSNAmyGGTCINIGCIPTKTLVHDAQQHTDFVRA------IQRKNEV-VNFLR 79
Cdd:PRK07845 5 VIIGGGPGGYEAALVAAQLGADVTVIERDGL--GGAAVLTDCVPSKTLIATAEVRTELRRAaelgirFIDDGEArVDLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 80 -NKNFHNLA-----DM------PNIDVIDGQAEFIN----NHSLRVHRPEANLE-IHGEKIFINTGAQ-----TVVPPIP 137
Cdd:PRK07845 83 vNARVKALAaaqsaDIrarlerEGVRVIAGRGRLIDpglgPHRVKVTTADGGEEtLDADVVLIATGASprilpTAEPDGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 138 GITTTPGVYDstgllnLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDII 217
Cdd:PRK07845 163 RILTWRQLYD------LDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 218 LNAHVERISHHENQVQVHSE--------HAQLAVdalliasGRQPATASLHPENAGIAVNERGAIVVDKQLHTTADNIWA 289
Cdd:PRK07845 237 KRSRAESVERTGDGVVVTLTdgrtvegsHALMAV-------GSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 290 MGDVTGGLQFTYISLDDYRIVRDELLGEGRRSTdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRAR 369
Cdd:PRK07845 310 AGDCTGVLPLASVAAMQGRIAMYHALGEAVSPL-RLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446969037 370 VMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:PRK07845 389 MSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSI 452
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
4-433 |
4.74e-27 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 113.56 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSnaMYGGTCINIGCIPTKTLVHDAQQH------------TDFV----RA 67
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKD--YLGGTCVNVGCVPKKIMFNAASIHdilensrhygfdTQFSfnlpLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 68 IQRKNEVVNFLRNKNFHNLADmPNIDVIDGQAEFINNHSL------------------RVHRPEANLE-------IHGEK 122
Cdd:PTZ00058 127 VERRDKYIRRLNDIYRQNLKK-DNVEYFEGKGSLLSENQVlikkvsqvdgeadesdddEVTIVSAGVSqlddgqvIEGKN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 123 IFINTGAQTVVPPIPGITTTpgvYDSTGLLNLKElPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIA 202
Cdd:PTZ00058 206 ILIAVGNKPIFPDVKGKEFT---ISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETII 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 203 DNIATILRDQGVDIILNAHVERISHHENQ---VQVHSEHAQLAVDALLIASGRQPATASLHPENAGIaVNERGAIVVDKQ 279
Cdd:PTZ00058 282 NELENDMKKNNINIITHANVEEIEKVKEKnltIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNI-KTPKGYIKVDDN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 280 LHTTADNIWAMGDVTG----------------------------------GLQFTYISLDDYRIVRDELLGEGRRSTdDR 325
Cdd:PTZ00058 361 QRTSVKHIYAVGDCCMvkknqeiedlnllklyneepylkkkentsgesyyNVQLTPVAINAGRLLADRLFGPFSRTT-NY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 326 KNVPYSVFMTPPLSRVGMTEEQARESGADIQVvtlpvaAIPRARVMNDTRGV------------LKAIVDNKTQRILGAS 393
Cdd:PTZ00058 440 KLIPSVIFSHPPIGTIGLSEQEAIDIYGKENV------KIYESRFTNLFFSVydmdpaqkektyLKLVCVGKEELIKGLH 513
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446969037 394 LLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
Cdd:PTZ00058 514 IVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
4-437 |
7.46e-26 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 110.39 E-value: 7.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQhtdfVRAIQRKNEVVNF-LRNKN 82
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDDSIGGTCVNVGCIPSKALLYATGK----YRELKNLAKLYTYgIYTNA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 83 FHN-----------LADMPNID----------VIDGQAEFINnHSLRVHRPEANLE----------------IHGEK--- 122
Cdd:PTZ00153 193 FKNgkndpvernqlVADTVQIDitklkeytqsVIDKLRGGIE-NGLKSKKFCKNSEhvqviyerghivdkntIKSEKsgk 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 123 ------IFINTGAqtvVPPIPGITTTPG--VYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFL 194
Cdd:PTZ00153 272 efkvknIIIATGS---TPNIPDNIEVDQksVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 195 PREDRDIADNIATI-LRDQGVDIILNAHVE--RISHHENQVQVHSEHAQLA----------------VDALLIASGRQPA 255
Cdd:PTZ00153 349 PLLDADVAKYFERVfLKSKPVRVHLNTLIEyvRAGKGNQPVIIGHSERQTGesdgpkknmndiketyVDSCLVATGRKPN 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 256 TASLHPENAGIAVNeRGAIVVDKQLHT------TADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGRRSTDDR---- 325
Cdd:PTZ00153 429 TNNLGLDKLKIQMK-RGFVSVDEHLRVlredqeVYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKENVNINvenw 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 326 -------KNVPYSVFMTPPLSRVGMTEEQARESGADIQV------------------VTLPVAAIPRA------RVMNDT 374
Cdd:PTZ00153 508 askpiiyKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVgveisfykanskvlcennISFPNNSKNNSynkgkyNTVDNT 587
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446969037 375 RGVLKAIVDNKTQRILGasLLCVDSHEMINIVKMVMDAGLPYSI--LRDQIFTHPSMSESLNDLF 437
Cdd:PTZ00153 588 EGMVKIVYLKDTKEILG--MFIVGSYASILIHEGVLAINLKLSVkdLAHMVHSHPTISEVLDAAF 650
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
90-295 |
7.66e-25 |
|
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: 104.12 E-value: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 90 PNIDVIDG-QAEFIN--NHSLRVHRPEanlEIHGEKIFINTGAQTVVPPIPGITTtPGVYDSTGLLNLKELPGHLGILGG 166
Cdd:COG0446 49 KGIDVRTGtEVTAIDpeAKTVTLRDGE---TLSYDKLVLATGARPRPPPIPGLDL-PGVFTLRTLDDADALREALKEFKG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 167 GYIG--------VEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERIsHHENQVQVHSEH 238
Cdd:COG0446 125 KRAVvigggpigLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAI-DGDDKVAVTLTD 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446969037 239 AQ-LAVDALLIASGRQPATASLhpENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTG 295
Cdd:COG0446 204 GEeIPADLVVVAPGVRPNTELA--KDAGLALGERGWIKVDETLQTSDPDVYAAGDCAE 259
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
4-437 |
1.09e-22 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 100.28 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVAL---IEQSNAM----YGGTCINIGCIPTK----------TLVHDAQQHTDFVR 66
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALfdyVKPSTQGtkwgLGGTCVNVGCVPKKlmhyaanigsIFHHDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 67 AIQRKNEVV----NFLRNKNFHNLADM--PNIDVIDGQAEFINNHSLRVHRPEANLEIHGEKIFINTGAQtvvPPIPgiT 140
Cdd:PTZ00052 86 SSFNWGKLVttvqNHIRSLNFSYRTGLrsSKVEYINGLAKLKDEHTVSYGDNSQEETITAKYILIATGGR---PSIP--E 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 141 TTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTIlEAASLFLPREDRDIADNIATILRDQGVDI 216
Cdd:PTZ00052 161 DVPGAKEysitSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV-AVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 217 ILNAHVERISHHENQVQV-HSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKQLhTTADNIWAMGDVTG 295
Cdd:PTZ00052 240 LEGVVPINIEKMDDKIKVlFSDGTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-TNIPNIFAVGDVVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 296 GL-QFTYISLDDYRIVRDELLGeGRRSTDDRKNVPYSVFMTPPLSRVGMTEEQARE--SGADIQVV-----TLPVAAIPR 367
Cdd:PTZ00052 319 GRpELTPVAIKAGILLARRLFK-QSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAkyGEDDIEEYlqefnTLEIAAVHR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 368 ARV-----------MNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
Cdd:PTZ00052 398 EKHerarkdeydfdVSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFMNL 477
|
.
gi 446969037 437 F 437
Cdd:PTZ00052 478 S 478
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
127-294 |
3.68e-18 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 85.96 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 127 TGAQTVVPPIPGITTtPGVY------DST-----------------GLLnlkelpghlgilgggyiGVEFASMFANFGSK 183
Cdd:COG1251 106 TGSRPRVPPIPGADL-PGVFtlrtldDADalraalapgkrvvviggGLI-----------------GLEAAAALRKRGLE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 184 VTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVH-SEHAQLAVDALLIASGRQPATASLhp 261
Cdd:COG1251 168 VTVVERAPRLLPRQlDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRlADGEELPADLVVVAIGVRPNTELA-- 245
|
170 180 190
....*....|....*....|....*....|...
gi 446969037 262 ENAGIAVNeRGaIVVDKQLHTTADNIWAMGDVT 294
Cdd:COG1251 246 RAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCA 276
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
117-292 |
3.28e-17 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 82.66 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 117 EIHGEKIFINTGAQTVVPPIPG----ITttpgvydstglLN-LKELPGHLGILGGGYI---------GVEFASMFANFGS 182
Cdd:PRK04965 97 QWQYDKLVLATGASAFVPPIPGrelmLT-----------LNsQQEYRAAETQLRDAQRvlvvgggliGTELAMDLCRAGK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 183 KVTILE-AASLF---LPREdrdIADNIATILRDQGVDIILNAHVERISHHENQVQVH-SEHAQLAVDALLIASGRQPATA 257
Cdd:PRK04965 166 AVTLVDnAASLLaslMPPE---VSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATlDSGRSIEVDAVIAAAGLRPNTA 242
|
170 180 190
....*....|....*....|....*....|....*
gi 446969037 258 sLHPEnAGIAVNeRGaIVVDKQLHTTADNIWAMGD 292
Cdd:PRK04965 243 -LARR-AGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
121-360 |
3.34e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 83.17 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 121 EKIFINTGAQTVVPPIPGITTTpGVYDSTGL---LNLKELPGHLGILGGGYI-----GVEFASMFANFGSKVTILEAASL 192
Cdd:PRK09564 105 DKLMIATGARPIIPPIKNINLE-NVYTLKSMedgLALKELLKDEEIKNIVIIgagfiGLEAVEAAKHLGKNVRIIQLEDR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 193 FLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIASGRQPATASLhpENAGIAVNER 271
Cdd:PRK09564 184 ILPDSfDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIVATGVKPNTEFL--EDTGLKTLKN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 272 GAIVVDKQLHTTADNIWAMGD-------VTGglQFTYISLDDY-----RIVRDELLGegrrstddrKNVPYSVFMTPP-- 337
Cdd:PRK09564 262 GAIIVDEYGETSIENIYAAGDcatiyniVSN--KNVYVPLATTanklgRMVGENLAG---------RHVSFKGTLGSAci 330
|
250 260
....*....|....*....|....*....
gi 446969037 338 ------LSRVGMTEEQARESGADIQVVTL 360
Cdd:PRK09564 331 kvldleAARTGLTEEEAKKLGIDYKTVFI 359
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
171-235 |
7.02e-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: 69.54 E-value: 7.02e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446969037 171 VEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVH 235
Cdd:pfam00070 12 LELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
4-296 |
4.91e-12 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 66.30 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAmyGG-----TCI-NIGCIPTKT----LVHDAQQHTdfvraiqrkne 73
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP--GGqlattKEIeNYPGFPEGIsgpeLAERLREQA----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 74 vvnflrnKNFhnladmpNIDVIDGQAEFI--NNHSLRVHRPEANlEIHGEKIFINTGAQTVVPPIPGIT--TTPGVY--- 146
Cdd:COG0492 68 -------ERF-------GAEILLEEVTSVdkDDGPFRVTTDDGT-EYEAKAVIIATGAGPRKLGLPGEEefEGRGVSyca 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 147 ------------------DStgllnlkelpghlgilgggyiGVEFASMFANFGSKVTILeaaslfLPREDRDIADNIATI 208
Cdd:COG0492 133 tcdgfffrgkdvvvvgggDS---------------------ALEEALYLTKFASKVTLI------HRRDELRASKILVER 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 209 LRD-QGVDIILNAHVERIsHHENQVQ-------VHSEHAQLAVDALLIASGRQPATASLhpENAGIAVNERGAIVVDKQL 280
Cdd:COG0492 186 LRAnPKIEVLWNTEVTEI-EGDGRVEgvtlknvKTGEEKELEVDGVFVAIGLKPNTELL--KGLGLELDEDGYIVVDEDM 262
|
330
....*....|....*.
gi 446969037 281 HTTADNIWAMGDVTGG 296
Cdd:COG0492 263 ETSVPGVFAAGDVRDY 278
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
183-293 |
6.09e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 63.61 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 183 KVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERIshHENQVQVHSEHaQLAVDALLIASGrqpATASLHPE 262
Cdd:COG1252 187 RITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEV--DADGVTLEDGE-EIPADTVIWAAG---VKAPPLLA 260
|
90 100 110
....*....|....*....|....*....|..
gi 446969037 263 NAGIAVNERGAIVVDKQLHTTA-DNIWAMGDV 293
Cdd:COG1252 261 DLGLPTDRRGRVLVDPTLQVPGhPNVFAIGDC 292
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
121-293 |
2.19e-07 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 53.29 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 121 EKIFINTGAQTVVPPIPGiTTTPGVY------DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFL 194
Cdd:TIGR02374 98 DKLILATGSYPFILPIPG-ADKKGVYvfrtieDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 195 PRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVH-SEHAQLAVDALLIASGRQPATaSLHPEnAGIAVNerG 272
Cdd:TIGR02374 177 AKQlDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRfKDGSSLEADLIVMAAGIRPND-ELAVS-AGIKVN--R 252
|
170 180
....*....|....*....|.
gi 446969037 273 AIVVDKQLHTTADNIWAMGDV 293
Cdd:TIGR02374 253 GIIVNDSMQTSDPDIYAVGEC 273
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
3-325 |
4.26e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 48.75 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVR-AIQRknevvnflrnk 81
Cdd:COG0665 2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNAGQLRPGLAALADRALVRLAReALDL----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 82 nFHNLADMPNIDVidgqaEFINNHSLRVHRPEANLEIHGEKIfintgaqtvvppipgitttpGVYDSTGlLNLKELPGHl 161
Cdd:COG0665 71 -WRELAAELGIDC-----DFRRTGVLYLARTEAELAALRAEA--------------------EALRALG-LPVELLDAA- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 162 gilgggyigvEFASMFANFGSKVTileAASLFLPRE---D-RDIADNIATILRDQGVDIILNAHVERISHHENQVQ-VHS 236
Cdd:COG0665 123 ----------ELREREPGLGSPDY---AGGLYDPDDghvDpAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTgVRT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 237 EHAQLAVDALLIASGrqPATASLHPEnAGIAVN---ERGAIvvdkqLHTTADNIWAMGDVTGGLQFTYISLDDYRIV--- 310
Cdd:COG0665 190 ERGTVRADAVVLAAG--AWSARLLPM-LGLRLPlrpVRGYV-----LVTEPLPDLPLRPVLDDTGVYLRPTADGRLLvgg 261
|
330
....*....|....*
gi 446969037 311 RDELLGEGRRSTDDR 325
Cdd:COG0665 262 TAEPAGFDRAPTPER 276
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
232-296 |
8.85e-06 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 47.68 E-value: 8.85e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446969037 232 VQVHSEHAQLAVDALLIASGRQPaTASLHPENAGIAVNERGAIVVDKQLHTTADNIWAMGDVTGG 296
Cdd:PRK12770 264 VPIPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTG 327
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
169-293 |
1.63e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 47.08 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 169 IGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQV-HSEHAQLAVDALl 247
Cdd:PRK13512 159 ISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSgKVEHYDMIIEGV- 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446969037 248 iasGRQPATASLhpENAGIAVNERGAIVVDKQLHTTADNIWAMGDV 293
Cdd:PRK13512 238 ---GTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDI 278
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-41 |
4.01e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 45.61 E-value: 4.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGG 41
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEK-NDTPGG 40
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
241-296 |
4.86e-05 |
|
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: 45.51 E-value: 4.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446969037 241 LAVDALLIASGRQPATASLhPENAGIAVNERGAIVVDKQ-LHTTADNIWAMGDVTGG 296
Cdd:COG0493 358 LPADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRG 413
|
|
| PRK07608 |
PRK07608 |
UbiH/UbiF family hydroxylase; |
3-34 |
6.23e-05 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181057 [Multi-domain] Cd Length: 388 Bit Score: 44.94 E-value: 6.23e-05
10 20 30
....*....|....*....|....*....|..
gi 446969037 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQ 34
Cdd:PRK07608 5 KFDVVVVGGGLVGASLALALAQSGLRVALLAP 36
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-35 |
1.49e-04 |
|
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: 43.77 E-value: 1.49e-04
10 20 30
....*....|....*....|....*....|....*
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQS 35
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERA 35
|
|
| ubiF |
PRK08020 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed |
2-35 |
3.56e-04 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
Pssm-ID: 181199 [Multi-domain] Cd Length: 391 Bit Score: 42.66 E-value: 3.56e-04
10 20 30
....*....|....*....|....*....|....
gi 446969037 2 NKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQS 35
Cdd:PRK08020 4 QPTDIAIVGGGMVGAALALGLAQHGFSVAVLEHA 37
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
181-279 |
1.31e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 40.67 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969037 181 GSKVTILEAASLFLPREDR-------DIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAV--DALLIASG 251
Cdd:pfam13738 178 GARVTVLYRGSEWEDRDSDpsyslspDTLNRLEELVKNGKIKAHFNAEVKEITEVDVSYKVHTEDGRKVTsnDDPILATG 257
|
90 100
....*....|....*....|....*...
gi 446969037 252 RQPATASLhpENAGIAVNERGAIVVDKQ 279
Cdd:pfam13738 258 YHPDLSFL--KKGLFELDEDGRPVLTEE 283
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
232-296 |
1.46e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 40.93 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446969037 232 VQVHSEHAQLAVDALLIASGrQPATASLHPENAGIAVNERGAIVVD-KQLHTTADNIWAMGDVTGG 296
Cdd:PRK11749 365 VPIEGSEFTLPADLVIKAIG-QTPNPLILSTTPGLELNRWGTIIADdETGRTSLPGVFAGGDIVTG 429
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
1-40 |
3.22e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 39.89 E-value: 3.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYG 40
Cdd:PRK06183 8 AHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTLYD 47
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
1-35 |
8.15e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 38.38 E-value: 8.15e-03
10 20 30
....*....|....*....|....*....|....*
gi 446969037 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQS 35
Cdd:PRK09126 1 MMHSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQ 35
|
|
| |
