|
Name |
Accession |
Description |
Interval |
E-value |
| HI0933_like |
pfam03486 |
HI0933-like protein; |
4-387 |
0e+00 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 560.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 4 FDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGGGRCNVTN-NGSLDNLLAGIPGNGRFLYSVFSQFDNH 82
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILISGGGRCNVTNlSEEPDNFLSRYPGNPKFLKSALSRFTPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 83 DIINFFTENGVKLKVEDHGRVFPASDKSRTIIEALEKKITELGGQVATQIEIVSVKKVDDQ-FVLKSADQTFTCEKLIVT 161
Cdd:pfam03486 81 DFIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKELGVKIRLRTRVLSVEKDDDGrFRVKTGGEELEADSLVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 162 TGGKSYPSTGSTGFGHEIARHFKHTITDLEAAESPLLTDFP---HKALQGISLDDVTLSYGKHVITH--DLLFTHFGLSG 236
Cdd:pfam03486 161 TGGLSWPKTGSTGFGYPLAEQFGHTIIPLRPALVPFTIDEPflfLKRLSGISLKNVVLSNGKGGITFrgELLFTHRGLSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 237 PAALRMSSFV------KGGEVLSLDVLPQLSEKDLVTFLEENRE----KSLKNALKTLLPERLAEFFVQ----GYPEKVK 302
Cdd:pfam03486 241 PAILQLSSYWrrailkKGGVTLSIDLLPDLDAEELAARLEKPRGahpkKSLKNSLAGLLPKRLAEFLLEqagiEPDKKLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 303 QLTEKEREQLVQSIKELKIPVTGKMSLAKSFVTKGGVSLKEINPKTLESKLVPGLHFAGEVMDINAHTGGFNITSALCTG 382
Cdd:pfam03486 321 QLSKKELAALAQLLKAWTFTPNGTEGYRTAEVTAGGVDTKELSSKTMESKKVPGLFFAGEVLDVDGWTGGYNLQWAWSSG 400
|
....*
gi 444285231 383 WVAGS 387
Cdd:pfam03486 401 YAAGQ 405
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
7-387 |
1.85e-180 |
|
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: 507.13 E-value: 1.85e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 7 IVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGGGRCNVTNNGSLDNLLAGIPGNGRFLYSVFSQFDNHDIIN 86
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKLLISGGGRCNLTNSCPTPEFVAYYPRNGKFLRSALSRFSNKDLID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 87 FFTENGVKLKVEDHGRVFPASDKSRTIIEALEKKITELGGQVATQIEIVSVKKVDDQFVLKSADQTFTCEKLIVTTGGKS 166
Cdd:TIGR00275 81 FFESLGLELKVEEDGRVFPCSDSAADVLDALLNELKELGVEILTNSKVKSIEKEDGGFGVETSGGEYEADKVIIATGGLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 167 YPSTGSTGFGHEIARHFKHTITDLEAAESPLLTDFP-HKALQGISLDDVTLSY--GKHVITH--DLLFTHFGLSGPAALR 241
Cdd:TIGR00275 161 YPQLGSTGDGYEIAESLGHTIVPPVPALVPLTLDESfLKELSGISLDGVVLSLvnGKKVLEEfgELLFTHFGLSGPAILD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 242 MSSFV------KGGEVLSLDVLPQLSEKDLVTFLEENRE----KSLKNALKTLLPERLAEFFVQGYP----EKVKQLTEK 307
Cdd:TIGR00275 241 LSAFAarallkHKGVELEIDLLPDLSEEELEQRLKRLRKsnpkKTVKNILKGLLPKRLAELLLEQLGidpdLPAAQLSKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 308 EREQLVQSIKELKIPVTGKMSLAKSFVTKGGVSLKEINPKTLESKLVPGLHFAGEVMDINAHTGGFNITSALCTGWVAGS 387
Cdd:TIGR00275 321 EIKKLVQLLKNWPFTISGTRGFKEAEVTAGGVSLKEINPKTMESKLVPGLYFAGEVLDIDGDTGGYNLQWAWSSGYLAGK 400
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
7-386 |
2.86e-177 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 499.19 E-value: 2.86e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 7 IVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGGGRCNVTNNGSLDNLLAGIPGNGRFLYSVFSQFDNHDIIN 86
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGRKILISGGGRCNFTNSEPLPEFLNYYGGNPHFLKSALSRFTPEDLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 87 FFTENGVKLKVEDHGRVFPASDKSRTIIEALEKKITELGGQVATQIEIVSVKKVDDQFVLKSAD-QTFTCEKLIVTTGGK 165
Cdd:COG2081 81 FFEGLGIETKEESSGRVFPDSSKASDILRALLAELREAGVEIRLRTRVTGIEKEDGGFGVETPDgETVRADAVVLATGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 166 SYPSTGSTGFGHEIARHFKHTITDLEAAESPL-LTDFPHKALQGISLDDVTLSYGKHVITH---DLLFTHFGLSGPAALR 241
Cdd:COG2081 161 SYPKLGSTGDGYRLAEQFGHTITPLRPALVPLtLSEHFFKRLAGLSLKNVALSVGGKKIASfrgELLFTHRGLSGPAILQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 242 MSSFV-----KGGEVLSLDVLPQLSEKDLVTFLEENRE----KSLKNALKTLLPERLAEFFVQGYPE--KVKQLTEKERE 310
Cdd:COG2081 241 LSSYWrdalkKGGATLTIDLLPDLDLEELDARLARPREkngkKSLKNVLRGLLPKRLAALLLELADPdkPLAQLSKKERE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285231 311 QLVQSIKELKIPVTGKMSLAKSFVTKGGVSLKEINPKTLESKLVPGLHFAGEVMDINAHTGGFNITSALCTGWVAG 386
Cdd:COG2081 321 ALAALLKAWPLTPTGTRGYDEAIVTAGGVDTKELDPKTMESKKVPGLYFAGEVLDVDGPTGGYNLQWAWSSGYAAG 396
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
4-163 |
1.20e-07 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 52.81 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 4 FDTIVIGGGPAGMMATISSSFYGQKTLLIEKnrklgkklaGTGGGRCNVTnngsldnllagipgngrflysvfsqfdnHD 83
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG---------GEPGGQLATT----------------------------KE 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 84 IINFFtenGvklkvedhgrvFPASDKSRTIIEALEKKITELGGQVATQiEIVSVKKVDDQFVLKSAD-QTFTCEKLIVTT 162
Cdd:COG0492 44 IENYP---G-----------FPEGISGPELAERLREQAERFGAEILLE-EVTSVDKDDGPFRVTTDDgTEYEAKAVIIAT 108
|
.
gi 444285231 163 G 163
Cdd:COG0492 109 G 109
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-180 |
8.81e-07 |
|
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: 50.60 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGkklaGT----GGGrCNVTNNG--------SLDN----LLAG 64
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG----GHtaaaQGG-INAAGTNvqkaagedSPEEhfydTVKG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 65 IPGNG------RFLysvfsqfDN-HDIINFFTENGVKLKVEDHGRV--FPASDKSRT----------IIEALEKKITELG 125
Cdd:COG1053 76 GDGLAdqdlveALA-------EEaPEAIDWLEAQGVPFSRTPDGRLpqFGGHSVGRTcyagdgtghaLLATLYQAALRLG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285231 126 GQVATQIEIVSVKKVDDQF---VLKSAD---QTFTCEKLIVTTGG------------------KSYPSTGSTGFGHEIA 180
Cdd:COG1053 149 VEIFTETEVLDLIVDDGRVvgvVARDRTgeiVRIRAKAVVLATGGfgrnyemraeylpeaegaLSTNAPGNTGDGIAMA 227
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-39 |
4.99e-06 |
|
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: 48.16 E-value: 4.99e-06
10 20 30
....*....|....*....|....*....|....*....
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLIEKnRKLG 39
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLG 38
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
5-64 |
5.90e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 47.99 E-value: 5.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 5 DTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKklAGTGGGRCNVTNNGSLDNLLAG 64
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG--MLTSGLVGPDMGFYLNKEQVVG 58
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-45 |
6.39e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 48.00 E-value: 6.39e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLIE--KNRKLGKKLAGT 45
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKGKPALGGT 48
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
3-179 |
6.67e-06 |
|
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: 48.02 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 3 HFDTIVIGGGPAGMMATISSSFYGQKTLLIEKnrklgKKLAGTgggrCnvTNNGSldnllagIPG----NGRFLYSVFSQ 78
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEK-----EYLGGT----C--LNVGC-------IPTkallHSAEVYDEIKH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 79 FDNHDIinffTENGVKLKVED-HGRVFPASDKSRTIIEALEK--KITELGGQ-VATQIEIVSVKKvddqfvlKSADQTFT 154
Cdd:TIGR01350 63 AKDLGI----EVENVSVDWEKmQKRKNKVVKKLVGGVSGLLKknKVTVIKGEaKFLDPGTVSVTG-------ENGEETLE 131
|
170 180
....*....|....*....|....*
gi 444285231 155 CEKLIVTTGGKSYPSTGSTGFGHEI 179
Cdd:TIGR01350 132 AKNIIIATGSRPRSLPGPFDFDGKV 156
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-39 |
3.28e-05 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 45.92 E-value: 3.28e-05
10 20 30
....*....|....*....|....*....|....*....
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLG 39
Cdd:PRK05249 3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVG 41
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
3-39 |
4.43e-05 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 45.14 E-value: 4.43e-05
10 20 30
....*....|....*....|....*....|....*..
gi 444285231 3 HFDTIVIGGGPAGMMATISSSFYGQKTLLIEKnRKLG 39
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLG 39
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-50 |
4.76e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 45.17 E-value: 4.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLIEKnrklgkklaGTGGGRC 50
Cdd:PRK06292 1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK---------GPLGGTC 41
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
5-103 |
1.45e-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: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 5 DTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGGGRC--NVTNNGSLDN-------LLAGIPGNGRFLYSV 75
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDalGNPPQGGIDSpelhptdTLKGLDELADHPYVE 80
|
90 100
....*....|....*....|....*...
gi 444285231 76 FSQFDNHDIINFFTENGVKLKVEDHGRV 103
Cdd:pfam00890 81 AFVEAAPEAVDWLEALGVPFSRTEDGHL 108
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-32 |
3.39e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 42.58 E-value: 3.39e-04
10 20 30
....*....|....*....|....*....|..
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLI 32
Cdd:PRK07494 5 KEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
5-166 |
7.54e-04 |
|
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: 41.16 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 5 DTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLgkklagTGGGRCNVTNNGSLDnLL--AGIpgngrfLYSVFSQFDNH 82
Cdd:pfam01494 3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHATT------SVLPRAHGLNQRTME-LLrqAGL------EDRILAEGVPH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 83 DIINFFTENG-VKLKVEDHGR-----VFPASDKSRTIIEALEkkitELGGQVATQIEIVSVKKVDD------QFVLKSAD 150
Cdd:pfam01494 70 EGMGLAFYNTrRRADLDFLTSpprvtVYPQTELEPILVEHAE----ARGAQVRFGTEVLSLEQDGDgvtavvRDRRDGEE 145
|
170
....*....|....*.
gi 444285231 151 QTFTCEKLIVTTGGKS 166
Cdd:pfam01494 146 YTVRAKYLVGCDGGRS 161
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
3-48 |
9.79e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 41.33 E-value: 9.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 444285231 3 HFDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGGG 48
Cdd:PRK12835 11 EVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGSTALSGGG 56
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
4-48 |
1.14e-03 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 40.79 E-value: 1.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 444285231 4 FDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGGG 48
Cdd:PRK07843 8 YDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGG 52
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
5-47 |
1.37e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 40.86 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 444285231 5 DTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGG 47
Cdd:PRK06134 14 DVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWSGG 56
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
1-32 |
1.86e-03 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 40.16 E-value: 1.86e-03
10 20 30
....*....|....*....|....*....|..
gi 444285231 1 MKhFDTIVIGGGPAGMMATISSSFYGQKTLLI 32
Cdd:COG3075 1 MK-FDVVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-36 |
2.40e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 39.80 E-value: 2.40e-03
10 20 30
....*....|....*....|....*....|....*.
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLIEKNR 36
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGL 38
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
4-48 |
2.56e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 39.74 E-value: 2.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 444285231 4 FDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGGG 48
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGGV 51
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-39 |
2.63e-03 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 39.83 E-value: 2.63e-03
10 20 30
....*....|....*....|....*....|....*....
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLG 39
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPG 39
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
304-386 |
2.95e-03 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 39.46 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 304 LTEKEREQLVQSIKelkipvtGkmsLAKSFVTKGGVSLKE--INP----KTLESKLVPGLHFAGevmDINAHTGgfnITS 377
Cdd:pfam01134 308 LPEDVQKRVLRTIP-------G---LENAEIVRPGYAIEYdyIDPpqllPTLETKKIPGLFFAG---QINGTEG---YEE 371
|
....*....
gi 444285231 378 ALCTGWVAG 386
Cdd:pfam01134 372 AAAQGLLAG 380
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
7-137 |
3.13e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 39.76 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 7 IVIGGGPAGMMATISSSFYGQKTLLIEKNRKLG----KKLAGTGG------GRCNVTNNGSL---DNLLAGIPGNG---- 69
Cdd:PTZ00306 413 IVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGgnsaKATSGINGwgtraqAKQDVLDGGKFferDTHLSGKGGHCdpgl 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285231 70 -RFLySVFSQfdnhDIINFFTENGVKLKV------EDHGRVFPASDKSR--------TIIEALEKKI-TELGGQVaTQIE 133
Cdd:PTZ00306 493 vKTL-SVKSA----DAISWLSSLGVPLTVlsqlggASRKRCHRAPDKKDgtpvpigfTIMRTLEDHIrTKLSGRV-TIMT 566
|
....
gi 444285231 134 IVSV 137
Cdd:PTZ00306 567 ETTV 570
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
8-43 |
3.23e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 39.46 E-value: 3.23e-03
10 20 30
....*....|....*....|....*....|....*.
gi 444285231 8 VIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLA 43
Cdd:COG1148 145 VIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAA 180
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
4-48 |
3.72e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 39.33 E-value: 3.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 444285231 4 FDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGGG 48
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSAGT 61
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
4-47 |
4.43e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 39.04 E-value: 4.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 444285231 4 FDTIVIGGGPAGMMATISSSFYGQKTLLIEKNRKLGKKLAGTGG 47
Cdd:PRK12839 9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGG 52
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-45 |
5.38e-03 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 38.60 E-value: 5.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 444285231 1 MKHFDTIVIGGGPAGMMATISSSFYGQKTLLIEknrklGKKLAGT 45
Cdd:PRK06116 2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIE-----AKRLGGT 41
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
2-35 |
8.23e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 37.91 E-value: 8.23e-03
10 20 30
....*....|....*....|....*....|....
gi 444285231 2 KHFDTIVIGGGPAGMMATISSSFYGQKTLLIEKN 35
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKG 34
|
|
|