|
Name |
Accession |
Description |
Interval |
E-value |
| Bthiol_YpdA |
TIGR04018 |
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ... |
5-321 |
0e+00 |
|
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 188533 [Multi-domain] Cd Length: 316 Bit Score: 510.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 5 ESIIIGGGPCGLSAAIEQKKKGIDTLVIEKGNIVDAIYHYPTHQTFFSSSDKLSIGDVPFIVEELKPRRNQALVYYREVV 84
Cdd:TIGR04018 1 DVIIIGAGPCGLACAIEAQKAGLSYLIIEKGNLVNSIYRYPTNMTFFSTSERLEIGGIPFISENPKPTRNEALEYYRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 85 KHHQLKVNAFEEVLTVKKMHDHFTLTTTKDVYQCRYLTVATGYYGQHNTLEVEGAELSKVMHYFKEPHPYFDQDVVIIGG 164
Cdd:TIGR04018 81 ERFKLNIRLYEEVLKVKKTDGGFEVTTEKGTYQAKNVIVATGYYDIPNLLNVPGEDLPKVSHYYKEAHPYFGQKVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 165 KNSAVDAAIELEKAGARVTVIYRGETYSPAIKPWILPNFESLVRRGNVQMHFNSQVTKITEDQVMFEK-EGETITIDNDY 243
Cdd:TIGR04018 161 SNSAVDAALELYRKGAEVTMVHRGDEVSSSVKYWVRPDIENRIKEGSIKAYFNSRVKEITEDSVTLETpDGEVHTIPNDF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504426777 244 VFAMIGYHPDYDFLQSIGIDIhtNEYGTAPVYNSETYETNIENCYIAGVIAAGNDANTIFIENGKYHGEAIARHILTK 321
Cdd:TIGR04018 241 VFALTGYRPDFEFLESLGVEL--DEDTGIPVYNPETMETNVPGLYLAGVIAAGMDTNKIFIENGRFHAPLIAEHIASK 316
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
13-291 |
9.83e-122 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 351.53 E-value: 9.83e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 13 PCGLSAAIEQKKKGIDT-LVIEKGNIVDAIYHYPTHQTFFSSSD---KLSIGDVPFIVEELKP---------RRNQALVY 79
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDyLILEKGNIGNSFYRYPTHMTFFSPSFtsnGFGIPDLNAISPGTSPaftfnrehpSGNEYAEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 80 YREVVKHHQLKVNAFEEVLTVKKMHDHFTLTTTKDVYQCRYLTVATGYYGQHNTLEVEgaELSKVMHYFKEPHPYFDQDV 159
Cdd:pfam13738 81 LRRVADHFELPINLFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATGEFDFPNKLGVP--ELPKHYSYVKDFHPYAGQKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 160 VIIGGKNSAVDAAIELEKAGARVTVIYRGE-------TYSPAIKPWILPNFESLVRRGNVQMHFNSQVTKITEDQVMFE- 231
Cdd:pfam13738 159 VVIGGYNSAVDAALELVRKGARVTVLYRGSewedrdsDPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKEITEVDVSYKv 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504426777 232 --KEGETITIDNDYVFAmIGYHPDYDFLQSIGIDIHTNEYgtaPVYNSETYETNIENCYIAG 291
Cdd:pfam13738 239 htEDGRKVTSNDDPILA-TGYHPDLSFLKKGLFELDEDGR---PVLTEETESTNVPGLFLAG 296
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
7-297 |
1.90e-42 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 148.73 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNIVDAIYHYPThqtffsssdklsIGDVPFIVEELKPrrnQALV-YYREVVK 85
Cdd:COG0492 4 VIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKE------------IENYPGFPEGISG---PELAeRLREQAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 86 HHQLKVnAFEEVLTVKKMHDHFTLTTTK-DVYQCRYLTVATGyyGQHNTLEVEGAELSKVM--HYFKEPHPYF--DQDVV 160
Cdd:COG0492 69 RFGAEI-LLEEVTSVDKDDGPFRVTTDDgTEYEAKAVIIATG--AGPRKLGLPGEEEFEGRgvSYCATCDGFFfrGKDVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 161 IIGGKNSAVDAAIELEKAGARVTVIYRGETYSPAikpwilpnfESLVRR----GNVQMHFNSQVTKITED----QVMFE- 231
Cdd:COG0492 146 VVGGGDSALEEALYLTKFASKVTLIHRRDELRAS---------KILVERlranPKIEVLWNTEVTEIEGDgrveGVTLKn 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504426777 232 -KEGETITIDNDYVFAMIGYHPDYDFLQSIGIDIhtNEYGTAPVynSETYETNIEncyiaGVIAAGN 297
Cdd:COG0492 217 vKTGEEKELEVDGVFVAIGLKPNTELLKGLGLEL--DEDGYIVV--DEDMETSVP-----GVFAAGD 274
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-318 |
1.92e-26 |
|
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: 108.03 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 1 MKTVESIIIGGGPCGLSAAIEQKKKGIDTLVIEKGnivDAI------YHYPThQTFFSSSDKLSIGDVPFI-VEELKPRR 73
Cdd:COG2072 4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKA---DDVggtwrdNRYPG-LRLDTPSHLYSLPFFPNWsDDPDFPTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 74 NQALVYYREVVKHHQLKVNAFEEVlTVKKMH-----DHFTLTTTK-DVYQCRYLTVATGYYGQHNTLEVEGAELSK--VM 145
Cdd:COG2072 80 DEILAYLEAYADKFGLRRPIRFGT-EVTSARwdeadGRWTVTTDDgETLTARFVVVATGPLSRPKIPDIPGLEDFAgeQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 146 H--YFKEPHPYFDQDVVIIGGKNSAVDAAIELEKAGARVTVIYRGETYS------------------------------- 192
Cdd:COG2072 159 HsaDWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRTPPWVlprpnydpergrpanylgleappalnrrdar 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 193 --------------------PAIKPW-----ILPNFESLVRRGNVQMHfNSQVTKITEDQVMFEkEGETITIDNdYVFAm 247
Cdd:COG2072 239 awlrrllraqvkdpelglltPDYPPGckrplLSTDYYEALRRGNVELV-TGGIERITEDGVVFA-DGTEHEVDV-IVWA- 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504426777 248 IGYHPDYDFLQSIGIdihtneYGTAPVYNSETYE----TNIENCYIAGVIAAGNDANTIF-IEngkYHGEAIARHI 318
Cdd:COG2072 315 TGFRADLPWLAPLDV------RGRDGRSGPRAYLgvvvPGFPNLFFLGPNSPSGHSSLTLgAE---RQARYIARLI 381
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
7-291 |
5.04e-24 |
|
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: 99.70 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNivdaiyHYPTHQTFFSSSdklsIGDVPFIVEELKpRRNQALVYYREVVKH 86
Cdd:pfam07992 4 VVIGGGPAGLAAALTLAQLGGKVTLIEDEG------TCPYGGCVLSKA----LLGAAEAPEIAS-LWADLYKRKEEVVKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 87 --HQLKVNAFEEVLTVKKMHDHFTLTTTKDV----YQCRYLTVATGyyGQHNTLEVEGAELskvmHYFKEPHPY------ 154
Cdd:pfam07992 73 lnNGIEVLLGTEVVSIDPGAKKVVLEELVDGdgetITYDRLVIATG--ARPRLPPIPGVEL----NVGFLVRTLdsaeal 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 155 ----FDQDVVIIGGKNSAVDAAIELEKAGARVTVIYRGE----TYSPAIKPWILPNFESLvrrgNVQMHFNSQVTKITED 226
Cdd:pfam07992 147 rlklLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDrllrAFDEEISAALEKALEKN----GVEVRLGTSVKEIIGD 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504426777 227 QVMFE-KEGETITIDNDYVFAMIGYHPDYDFLQSIGIDihTNEYGTAPVynSETYETNIENCYIAG 291
Cdd:pfam07992 223 GDGVEvILKDGTEIDADLVVVAIGRRPNTELLEAAGLE--LDERGGIVV--DEYLRTSVPGIYAAG 284
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-326 |
8.62e-18 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 83.69 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 1 MKTVESIIIGGGPCGLSAAIEQKKKGIDTLVIEKGN----------------IVDA-IYHYPTH-QTFFSSSDKLSIgDV 62
Cdd:PRK06292 1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclnvgcipskalIAAAeAFHEAKHaEEFGIHADGPKI-DF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 63 PFIVEELKPRRNqalvyyrEVVKHHQLKVNAFEEVLTVKK----MHDHfTLTTTKDVYQCRYLTVATGyygqHNTLEVEG 138
Cdd:PRK06292 80 KKVMARVRRERD-------RFVGGVVEGLEKKPKIDKIKGtarfVDPN-TVEVNGERIEAKNIVIATG----SRVPPIPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 139 AELSKVMHYF---------KEPhpyfdQDVVIIGGknsavdAAIELEKA------GARVTVIYRGETyspaikpwILPNF 203
Cdd:PRK06292 148 VWLILGDRLLtsddafeldKLP-----KSLAVIGG------GVIGLELGqalsrlGVKVTVFERGDR--------ILPLE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 204 ESLVRR-------GNVQMHFNSQVTKITEDQ----VMFEKEGETITIDNDYVFAMIGYHPDYDFLQSIGIDIHTNEYGTa 272
Cdd:PRK06292 209 DPEVSKqaqkilsKEFKIKLGAKVTSVEKSGdekvEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGR- 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 504426777 273 PVYNsETYETNIENCYIAGviaagnDANTI--FIENGKYHGEAIARHILTKKQSPL 326
Cdd:PRK06292 288 PVVD-EHTQTSVPGIYAAG------DVNGKppLLHEAADEGRIAAENAAGDVAGGV 336
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
123-291 |
8.07e-14 |
|
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: 71.70 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 123 VATGYyGQHNTLEVEGAELSKVM-----------HYFKEPHPYFDQDVVIIGGKNSAVDAAIELEKAGAR-VTVIYR-GE 189
Cdd:COG0493 212 LATGA-GKPRDLGIPGEDLKGVHsamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAEsVTIVYRrTR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 190 TYSPAIKpwilpnFE-SLVRRGNVQMHFNSQVTKITED-----------------------QVMFEKEGETITIDNDYVF 245
Cdd:COG0493 291 EEMPASK------EEvEEALEEGVEFLFLVAPVEIIGDengrvtglecvrmelgepdesgrRRPVPIEGSEFTLPADLVI 364
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504426777 246 AMIGYHPDYDFLQSIgIDIHTNEYGTAPVyNSETYETNIENCYIAG 291
Cdd:COG0493 365 LAIGQTPDPSGLEEE-LGLELDKRGTIVV-DEETYQTSLPGVFAGG 408
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
7-327 |
1.11e-13 |
|
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: 71.27 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNI---------------VDA--IYHYPTHQTFFSssdkLSIGDVPFIVEEL 69
Cdd:COG1249 7 VVIGAGPGGYVAAIRAAQLGLKVALVEKGRLggtclnvgcipskalLHAaeVAHEARHAAEFG----ISAGAPSVDWAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 70 KPRRNQ---ALV-YYREVVKHHqlKVNAFEEVLTVKKMHdhfTLT-TTKDVYQCRYLTVATGyyGQHNTLEVEGaelskv 144
Cdd:COG1249 83 MARKDKvvdRLRgGVEELLKKN--GVDVIRGRARFVDPH---TVEvTGGETLTADHIVIATG--SRPRVPPIPG------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 145 mhyFKEPHPY-----FDQD-----VVIIGGknsavdAAIELE------KAGARVTVIYRGETyspaikpwILPNF----- 203
Cdd:COG1249 150 ---LDEVRVLtsdeaLELEelpksLVVIGG------GYIGLEfaqifaRLGSEVTLVERGDR--------LLPGEdpeis 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 204 ----ESLVRRGnVQMHFNSQVTKITED----QVMFEKEGETITIDNDYVFAMIGYHPDydfLQSIGID---IHTNEYGTA 272
Cdd:COG1249 213 ealeKALEKEG-IDILTGAKVTSVEKTgdgvTVTLEDGGGEEAVEADKVLVATGRRPN---TDGLGLEaagVELDERGGI 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 504426777 273 PVynSETYETNIENCYIAG-VIAAGNDANTifienGKYHGEAIARHILTKKQSPLE 327
Cdd:COG1249 289 KV--DEYLRTSVPGIYAIGdVTGGPQLAHV-----ASAEGRVAAENILGKKPRPVD 337
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
63-319 |
2.20e-13 |
|
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: 69.84 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 63 PFIVEELKPRRNQALVYYREVVKHHQLKVNAFEEVLTV----KKMHdhftlTTTKDVYQCRYLTVATGyyGQHNTLEVEG 138
Cdd:COG0446 25 PYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIdpeaKTVT-----LRDGETLSYDKLVLATG--ARPRPPPIPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 139 AELSKVMH------------YFKEPHPyfdQDVVIIGGKNSAVDAAIELEKAGARVTVIYRGETYSPAIKPWILPNFESL 206
Cdd:COG0446 98 LDLPGVFTlrtlddadalreALKEFKG---KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 207 VRRGNVQMHFNSQVTKITED---QVMFEkEGEtiTIDNDYVFAMIGYHPDYDFLQSIGIDIHTNeyGTAPVynSETYETN 283
Cdd:COG0446 175 LREHGVELRLGETVVAIDGDdkvAVTLT-DGE--EIPADLVVVAPGVRPNTELAKDAGLALGER--GWIKV--DETLQTS 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 504426777 284 IENCYIAGviaagnD-ANTIFIENGKY-----------HGEAIARHIL 319
Cdd:COG0446 248 DPDVYAAG------DcAEVPHPVTGKTvyiplasaankQGRVAAENIL 289
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
8-323 |
2.64e-11 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 64.04 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 8 IIGGGPCGLSAAIEQKKKGidtlviekgnivdaiyhyptHQ-TFFSSSDKlsIGDVpfiveelkprrnqaLVY----YRE 82
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKG--------------------YDvTIFEARDK--AGGL--------------LRYgipeFRL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 83 VVKHhqlkvnAFEEVLTVKKM-----HDH-----FTLTTTKDVYQCRYLtvATGYYGQhNTLEVEGAELSKVMH---YFK 149
Cdd:PRK11749 189 PKDI------VDREVERLLKLgveirTNTevgrdITLDELRAGYDAVFI--GTGAGLP-RFLGIPGENLGGVYSavdFLT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 150 EP---HPYFD----QDVVIIGGKNSAVDAAIELEKAGAR-VTVIYR-GETYSPAIKpwilpnFE-SLVRRGNVQMHFNSQ 219
Cdd:PRK11749 260 RVnqaVADYDlpvgKRVVVIGGGNTAMDAARTAKRLGAEsVTIVYRrGREEMPASE------EEvEHAKEEGVEFEWLAA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 220 VTKITED-----QVMFEK----------------EGETITIDNDYVFAMIGYHPDYDFLQSIGiDIHTNEYGTaPVYNSE 278
Cdd:PRK11749 334 PVEILGDegrvtGVEFVRmelgepdasgrrrvpiEGSEFTLPADLVIKAIGQTPNPLILSTTP-GLELNRWGT-IIADDE 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 504426777 279 TYETNIENCYIAGVIAAGnDANTIF-IENGKYHGEAIARHILTKKQ 323
Cdd:PRK11749 412 TGRTSLPGVFAGGDIVTG-AATVVWaVGDGKDAAEAIHEYLEGAAS 456
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
7-126 |
6.03e-09 |
|
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: 56.84 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNIV---------------------DAIYHYPTHQTF-------FSSSDKL- 57
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIgkkllisgggrcnltnscptpEFVAYYPRNGKFlrsalsrFSNKDLId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 58 ---SIGdVPFIVEE---LKPRRNQAlvyyREVVKH-----HQLKVNAF--EEVLTVKKMHDHFTLTTTKDVYQCRYLTVA 124
Cdd:TIGR00275 81 ffeSLG-LELKVEEdgrVFPCSDSA----ADVLDAllnelKELGVEILtnSKVKSIEKEDGGFGVETSGGEYEADKVIIA 155
|
..
gi 504426777 125 TG 126
Cdd:TIGR00275 156 TG 157
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
159-228 |
4.84e-08 |
|
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: 49.51 E-value: 4.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 159 VVIIGGKNSAVDAAIELEKAGARVTVIYRGETYSPAIKPWILPNFESLVRRGNVQMHFNSQVTKITEDQV 228
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGD 71
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
1-291 |
1.16e-07 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 52.74 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 1 MKTvesIIIGGGPCGLSAAIEQKK--KGIDTLVIEKGNIVdaiyhypthqtffsssdklSIG--DVPFIVEELKPRRNQA 76
Cdd:PRK09564 1 MKI---IIIGGTAAGMSAAAKAKRlnKELEITVYEKTDIV-------------------SFGacGLPYFVGGFFDDPNTM 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 77 LVYYREV---------VKHHQLKVNAFEEVLTVKKMHdhftlttTKDVYQCRY--LTVATG---------------YYGQ 130
Cdd:PRK09564 59 IARTPEEfiksgidvkTEHEVVKVDAKNKTITVKNLK-------TGSIFNDTYdkLMIATGarpiippikninlenVYTL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 131 HNTleVEGAELSKVMhyfKEPHpyfDQDVVIIGGKNSAVDAAIELEKAGARVTVIYR-----GETYSPAIKPWIlpnfES 205
Cdd:PRK09564 132 KSM--EDGLALKELL---KDEE---IKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLedrilPDSFDKEITDVM----EE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 206 LVRRGNVQMHFNSQVTKITedqvmFEKEGETITIDN-----DYVFAMIGYHPDYDFLQSIGID------IHTNEYGtapv 274
Cdd:PRK09564 200 ELRENGVELHLNEFVKSLI-----GEDKVEGVVTDKgeyeaDVVIVATGVKPNTEFLEDTGLKtlkngaIIVDEYG---- 270
|
330
....*....|....*..
gi 504426777 275 ynsetyETNIENCYIAG 291
Cdd:PRK09564 271 ------ETSIENIYAAG 281
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
7-228 |
1.25e-07 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 52.37 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVI---EKG---NIVDAIYHYPTHQTFFSSsdklsigdvPFIVEELkprRNQALVYY 80
Cdd:PRK10262 10 LILGSGPAGYTAAVYAARANLQPVLItgmEKGgqlTTTTEVENWPGDPNDLTG---------PLLMERM---HEHATKFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 81 REVVkhhqlkvnaFEEVLTVKKMHDHFTLTTTKDVYQCRYLTVATGYYGQHNTLEVEGAELSKVMHYFKEPHPYF--DQD 158
Cdd:PRK10262 78 TEII---------FDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFyrNQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 159 VVIIGGKNSAVDAAIELEKAGARVTVIYRGETYSPaiKPWILPNFESLVRRGNVQMHFNSQVTKITEDQV 228
Cdd:PRK10262 149 VAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRA--EKILIKRLMDKVENGNIILHTNRTLEEVTGDQM 216
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
7-301 |
2.25e-07 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 52.08 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDT-LVIEK-GNIVdaiyhypthqtffssSDKLSIGDVPFIVEELKPRRNQALvyyREVV 84
Cdd:PRK15317 215 LVVGGGPAGAAAAIYAARKGIRTgIVAERfGGQV---------------LDTMGIENFISVPETEGPKLAAAL---EEHV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 85 KHHQLKVNAFEEVLTVKKMHDHFTLTTTKD-VYQCRYLTVATGyyGQHNTLEVEGAE--LSKVMHYFkePH---PYF-DQ 157
Cdd:PRK15317 277 KEYDVDIMNLQRASKLEPAAGLIEVELANGaVLKAKTVILATG--ARWRNMNVPGEDeyRNKGVAYC--PHcdgPLFkGK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 158 DVVIIGGKNSAVDAAIELekAG--ARVTVIYRGETyspaikpwiLPNFESLVRR----GNVQMHFNSQVTKITEDQvmfE 231
Cdd:PRK15317 353 RVAVIGGGNSGVEAAIDL--AGivKHVTVLEFAPE---------LKADQVLQDKlrslPNVTIITNAQTTEVTGDG---D 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 232 K----------EGETITIDNDYVFAMIGYHPDYDFLQSIgidIHTNEYGTAPVynSETYETNIEncyiaGVIAAGnDANT 301
Cdd:PRK15317 419 KvtgltykdrtTGEEHHLELEGVFVQIGLVPNTEWLKGT---VELNRRGEIIV--DARGATSVP-----GVFAAG-DCTT 487
|
|
| PRK06126 |
PRK06126 |
hypothetical protein; Provisional |
1-98 |
2.84e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235704 [Multi-domain] Cd Length: 545 Bit Score: 48.84 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 1 MKTVES--IIIGGGPCGLSAAIEQKKKGIDTLVIE---------KGN--------------IVDAIYH------YPTHQT 49
Cdd:PRK06126 3 ENTSETpvLIVGGGPVGLALALDLGRRGVDSILVErkdgtafnpKANttsarsmehfrrlgIADEVRSaglpvdYPTDIA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504426777 50 FFSSSDKLSIG--DVPFIVEELKPRRNQAlVYYREVVKHHQLKVNAFEEVL 98
Cdd:PRK06126 83 YFTRLTGYELArfRLPSAREAITPVGGPD-GSWPSPELPHRIPQKYLEPIL 132
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
7-126 |
1.10e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 46.81 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNIV----------------------DAIYHYPTHQTFFSSSdkLSIGD--- 61
Cdd:pfam03486 4 IVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLgrkilisgggrcnvtnlseepdNFLSRYPGNPKFLKSA--LSRFTpwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 62 ---------VPFIVEE---LKPRRNQAlvyyREVVK---------HHQLKVNAfeEVLTVKKMHDH-FTLTTTKDVYQCR 119
Cdd:pfam03486 82 fiaffeslgVPLKEEDhgrLFPDSDKA----SDIVDallnelkelGVKIRLRT--RVLSVEKDDDGrFRVKTGGEELEAD 155
|
....*..
gi 504426777 120 YLTVATG 126
Cdd:pfam03486 156 SLVLATG 162
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
1-81 |
1.97e-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: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 1 MKTVesIIIGGGPCGLSAAIEQKKKGIDTLVIEK--------------GNIVDAIYHypthqTFFSSS-------DKLSI 59
Cdd:COG1232 1 MKRV--AVIGGGIAGLTAAYRLAKAGHEVTVLEAsdrvgglirtvevdGFRIDRGPH-----SFLTRDpevlellRELGL 73
|
90 100
....*....|....*....|..
gi 504426777 60 GDvpfivEELKPRRNQALVYYR 81
Cdd:COG1232 74 GD-----ELVWPNTRKSYIYYG 90
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
158-318 |
3.46e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 44.98 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 158 DVVIIGGKNSAVDAAIELEKAGA-RVTVIY-RGETYSPAIKPWIlpnfESLVRRGNVQMHFNSQVTKITEDQV---MFEK 232
Cdd:PRK12770 174 KVVVVGAGLTAVDAALEAVLLGAeKVYLAYrRTINEAPAGKYEI----ERLIARGVEFLELVTPVRIIGEGRVegvELAK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 233 -----------------EGETITIDNDYVFAMIGYHPDYDFLQSiGIDIHTNEYGTAPVynSETYETNIENCYIAGVIAA 295
Cdd:PRK12770 250 mrlgepdesgrprpvpiPGSEFVLEADTVVFAIGEIPTPPFAKE-CLGIELNRKGEIVV--DEKHMTSREGVFAAGDVVT 326
|
170 180
....*....|....*....|...
gi 504426777 296 GNDantiFIENGKYHGEAIARHI 318
Cdd:PRK12770 327 GPS----KIGKAIKSGLRAAQSI 345
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
7-34 |
6.03e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 44.44 E-value: 6.03e-05
10 20
....*....|....*....|....*...
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEK 34
Cdd:COG1053 7 VVVGSGGAGLRAALEAAEAGLKVLVLEK 34
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-34 |
6.14e-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: 44.16 E-value: 6.14e-05
10 20 30
....*....|....*....|....*....|....
gi 504426777 1 MKTVESIIIGGGPCGLSAAIEQKKKGIDTLVIEK 34
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVER 34
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
7-39 |
9.92e-05 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 43.95 E-value: 9.92e-05
10 20 30
....*....|....*....|....*....|...
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNIVD 39
Cdd:COG2509 34 VIVGAGPAGLFAALELAEAGLKPLVLERGKDVE 66
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
4-34 |
9.92e-05 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 43.47 E-value: 9.92e-05
10 20 30
....*....|....*....|....*....|.
gi 504426777 4 VESIIIGGGPCGLSAAIEQKKKGIDTLVIEK 34
Cdd:pfam01494 2 TDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
7-53 |
1.35e-04 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 43.43 E-value: 1.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGnivdaiyHYPTHQTFFSS 53
Cdd:pfam00890 3 LVIGGGLAGLAAALAAAEAGLKVAVVEKG-------QPFGGATAWSS 42
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
158-244 |
1.46e-04 |
|
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: 43.08 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 158 DVVIIGGKNSAVDAAIELEKAGARVTVIYRGETYS---PAIKPWIL---------PNFESLVRR---------GNVQMHF 216
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPyggCVLSKALLgaaeapeiaSLWADLYKRkeevvkklnNGIEVLL 81
|
90 100 110
....*....|....*....|....*....|..
gi 504426777 217 NSQVTKITEDQVMFE----KEGETITIDNDYV 244
Cdd:pfam07992 82 GTEVVSIDPGAKKVVleelVDGDGETITYDRL 113
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
8-38 |
1.59e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 39.44 E-value: 1.59e-04
10 20 30
....*....|....*....|....*....|.
gi 504426777 8 IIGGGPCGLSAAIEQKKKGIDTLVIEKGNIV 38
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRL 31
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
1-57 |
2.06e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 42.95 E-value: 2.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504426777 1 MKTVESIIIGGGPCGLSAAIEQKKKGIDTLVIEKGNIVDAIYHYPTHQ---------TFFSSSDKL 57
Cdd:PRK07208 2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKgnrfdigghRFFSKSPEV 67
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
8-275 |
4.22e-04 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 41.77 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 8 IIGGGPCGLSAAIEQKKKGIDTLVIEKGNIVDAIYHY------------PT----HQTFFSS------SDKLSIGDVPFI 65
Cdd:PLN02172 15 VIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYtpksesdplsldPTrsivHSSVYESlrtnlpRECMGYRDFPFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 66 V----EELKPRRNQAlvyYREVVKHHQLKVNAFE---------EVLTVKKMHDHFTLTTTK-------DVYQCryLTVAT 125
Cdd:PLN02172 95 PrfddESRDSRRYPS---HREVLAYLQDFAREFKieemvrfetEVVRVEPVDGKWRVQSKNsggfskdEIFDA--VVVCN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 126 GYYGQHNTLEVEGAEL--SKVMHY--FKEPHPYFDQDVVIIGGKNSAVDAAIELEKAGARVTVIYRG---ETYSPaikpw 198
Cdd:PLN02172 170 GHYTEPNVAHIPGIKSwpGKQIHShnYRVPDPFKNEVVVVIGNFASGADISRDIAKVAKEVHIASRAsesDTYEK----- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504426777 199 iLPnfeslVRRGNVQMHfnSQVTKITEDQVMFEKEGETITIDNdyVFAMIGYHPDYDFLQSIGIdIHTNEYGTAPVY 275
Cdd:PLN02172 245 -LP-----VPQNNLWMH--SEIDTAHEDGSIVFKNGKVVYADT--IVHCTGYKYHFPFLETNGY-MRIDENRVEPLY 310
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-38 |
6.34e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 41.37 E-value: 6.34e-04
10 20 30
....*....|....*....|....*....|....*...
gi 504426777 1 MKTVESIIIGGGPCGLSAAIEQKKKGIDTLVIEKGNIV 38
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTP 38
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
3-34 |
7.59e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 41.22 E-value: 7.59e-04
10 20 30
....*....|....*....|....*....|..
gi 504426777 3 TVESIIIGGGPCGLSAAIEQKKKGIDTLVIEK 34
Cdd:PRK12842 9 TCDVLVIGSGAGGLSAAITARKLGLDVVVLEK 40
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
8-45 |
9.37e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 40.66 E-value: 9.37e-04
10 20 30
....*....|....*....|....*....|....*...
gi 504426777 8 IIGGGPCGLSAAIEQKKKGIDTLVIEKgniVDAIYHYP 45
Cdd:PRK06183 15 IVGAGPVGLTLANLLGQYGVRVLVLER---WPTLYDLP 49
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
7-37 |
1.99e-03 |
|
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: 39.22 E-value: 1.99e-03
10 20 30
....*....|....*....|....*....|.
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNI 37
Cdd:TIGR02032 4 VVVGAGPAGASAAYRLADKGLRVLLLEKKSF 34
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
123-298 |
2.29e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 39.38 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 123 VATGYYGQhNTLEVEGAELSKV---MHYFK---------EPHPYFD---QDVVIIGGKNSAVDA---AIELekaGARvTV 184
Cdd:PRK12810 234 LGTGAYKP-RDLGIPGRDLDGVhfaMDFLIqntrrvlgdETEPFISakgKHVVVIGGGDTGMDCvgtAIRQ---GAK-SV 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 185 IYRGETYSPA---IKPWILPNFESLVRRGN-----VQMHFNSQVTKI--------------TEDQV--MFEKEGETITID 240
Cdd:PRK12810 309 TQRDIMPMPPsrrNKNNPWPYWPMKLEVSNaheegVEREFNVQTKEFegengkvtgvkvvrTELGEgdFEPVEGSEFVLP 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504426777 241 NDYVFAMIGY-HPDYDFLQSIGIDihTNEYGTApVYNSETYETNIENCYIAGVIAAGND 298
Cdd:PRK12810 389 ADLVLLAMGFtGPEAGLLAQFGVE--LDERGRV-AAPDNAYQTSNPKVFAAGDMRRGQS 444
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
156-187 |
2.43e-03 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 39.82 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|..
gi 504426777 156 DQDVVIIGGKNSAVDAAIELEKAGARVTVIYR 187
Cdd:PRK12779 447 GKEVFVIGGGNTAMDAARTAKRLGGNVTIVYR 478
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
159-261 |
2.67e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 39.47 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 159 VVIIGGKNSAVDAAIELEKAGA-RVTVIYRgetySPAIKPWILPN-FESLVRRGnVQMHFNSQVTKITED---------- 226
Cdd:PRK12771 270 VVVIGGGNTAMDAARTARRLGAeEVTIVYR----RTREDMPAHDEeIEEALREG-VEINWLRTPVEIEGDengatglrvi 344
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 504426777 227 -QVMFEK---------EGETITIDNDYVFAMIGYHPDYDFLQSIG 261
Cdd:PRK12771 345 tVEKMELdedgrpspvTGEEETLEADLVVLAIGQDIDSAGLESVP 389
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
161-296 |
3.65e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 38.96 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426777 161 IIGGKNSAVDAAIELEKAGARVTVIYRGETYSPAIKPWILPNFESLVRRGNVQMHFNSQVTKIT--EDQVMFEKEGETIT 238
Cdd:PRK07251 162 IIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKndGDQVLVVTEDETYR 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 504426777 239 IDNdYVFAMiGYHPDYDFLQSIGIDIHTNEYGTAPVynSETYETNIENCYIAGVIAAG 296
Cdd:PRK07251 242 FDA-LLYAT-GRKPNTEPLGLENTDIELTERGAIKV--DDYCQTSVPGVFAVGDVNGG 295
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
3-35 |
3.81e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 39.02 E-value: 3.81e-03
10 20 30
....*....|....*....|....*....|...
gi 504426777 3 TVESIIIGGGPCGLSAAIEQKKKGIDTLVIEKG 35
Cdd:PRK12835 11 EVDVLVVGSGGGGMTAALTAAARGLDTLVVEKS 43
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
1-34 |
3.82e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 38.70 E-value: 3.82e-03
10 20 30
....*....|....*....|....*....|....*
gi 504426777 1 MKTVESI-IIGGGPCGLSAAIEQKKKGIDTLVIEK 34
Cdd:PRK06847 1 MAAVKKVlIVGGGIGGLSAAIALRRAGIAVDLVEI 35
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
8-56 |
4.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 38.71 E-value: 4.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504426777 8 IIGGGPCGLSAAIEQKKKGIDTLVIEK--------------GNIVDAIYHypthqtFFSSSDK 56
Cdd:PRK07233 4 IVGGGIAGLAAAYRLAKRGHEVTVFEAddqlgglaasfefgGLPIERFYH------HIFKSDE 60
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
7-38 |
5.83e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 38.15 E-value: 5.83e-03
10 20 30
....*....|....*....|....*....|..
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNIV 38
Cdd:pfam01266 3 VVIGGGIVGLSTAYELARRGLSVTLLERGDDP 34
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
7-37 |
6.10e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 37.96 E-value: 6.10e-03
10 20 30
....*....|....*....|....*....|.
gi 504426777 7 IIIGGGPCGLSAAIEQKKKGIDTLVIEKGNI 37
Cdd:COG0665 6 VVIGGGIAGLSTAYHLARRGLDVTVLERGRP 36
|
|
| PRK08626 |
PRK08626 |
fumarate reductase flavoprotein subunit; Provisional |
1-32 |
7.31e-03 |
|
fumarate reductase flavoprotein subunit; Provisional
Pssm-ID: 181507 [Multi-domain] Cd Length: 657 Bit Score: 38.03 E-value: 7.31e-03
10 20 30
....*....|....*....|....*....|....
gi 504426777 1 MKTV--ESIIIGGGPCGLSAAIEQKKKGIDTLVI 32
Cdd:PRK08626 1 MKIIytDALVIGAGLAGLRVAIAAAQRGLDTIVL 34
|
|
| |
