|
Name |
Accession |
Description |
Interval |
E-value |
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
2-477 |
0e+00 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 720.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 2 IRFLINKDLIELDDARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLGEVNNDGsaLHYRTVNSCITLMSAVHGKQL 81
Cdd:COG4630 1 IRFLLNGELVELSDVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVGELDDGG--LRYRAVNACILFLPQLDGKAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 82 IAVEHLAD-EGTLHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQ 160
Cdd:COG4630 79 VTVEGLAGpDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAARAMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 161 GEAADHFAKTASNTLAKLKDIQDNAGTAI--GSSGVIMPTSREELANAIQGYPAAPLVAGSTDFGLSITQQLKNVEKVIN 238
Cdd:COG4630 159 APAPDPFAADRAAVAAALRALADGETVELgaGGSRFLAPATLDELAALLAAHPDARLVAGATDVGLWVTKQLRDLPPVIF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 239 LSAMDSLKKCTKTEQALIIGAGAPLNDIASPLLSAFPQLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRAS 318
Cdd:COG4630 239 LGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAHFPELAELLRRFASRQIRNAGTLGGNIANGSPIGDSPPALIALGAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 319 LHLDNGQQVRVIPLKGFFTGYRQTQLEKGEWISAIEIPLLSKDNNVAAYKISKRMEDDISAVCAVFNLTLVDGVVTSLQT 398
Cdd:COG4630 319 LVLRSGDGRRTLPLEDFFLGYRKTDLQPGEFVEAIRIPLPAAGQRLRAYKVSKRFDDDISAVCAAFALTLDDGTVTEARI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763177138 399 GFGGVAATPETCPTLERALIGKQWqSADCLHLGKQMLKDAFNPIDDVRASAAYRNQVLSNLWHRFWLEKQAQNTiETRV 477
Cdd:COG4630 399 AFGGMAATPKRARAAEAALLGQPW-TEATVAAAAAALAQDFTPLSDMRASAEYRLAVAANLLRRFFLETQGEAP-ATRV 475
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
2-466 |
0e+00 |
|
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 274365 [Multi-domain] Cd Length: 467 Bit Score: 580.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 2 IRFLINKDLIELDDARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLGEVNNDGSaLHYRTVNSCITLMSAVHGKQL 81
Cdd:TIGR02963 1 IRFFLNGETVTLSDVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVGELVDGGK-LRYRSVNACIQFLPSLDGKAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 82 IAVEHLAD-EGTLHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQ 160
Cdd:TIGR02963 80 VTVEDLRQpDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPILDAAEAAFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 161 GEAADHFAKTASNTLAKLKDIQDNAGTAIGSSG--VIMPTSREELANAIQGYPAAPLVAGSTDFGLSITQQLKNVEKVIN 238
Cdd:TIGR02963 160 YPCSDPLDADRAPIIERLRALRAGETVELNFGGerFIAPTTLDDLAALKAAHPDARIVAGSTDVGLWVTKQMRDLPDVIY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 239 LSAMDSLKKCTKTEQALIIGAGAPLNDIASPLLSAFPQLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRAS 318
Cdd:TIGR02963 240 VGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPELGELLRRFASLQIRNAGTLGGNIANGSPIGDSPPALIALGAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 319 LHLDNGQQVRVIPLKGFFTGYRQTQLEKGEWISAIEIPLLSKDNNVAAYKISKRMEDDISAVCAVFNLTLVDGVVTSLQT 398
Cdd:TIGR02963 320 LTLRKGEGRRTLPLEDFFIDYGKTDRQPGEFVEALHVPRPTPGERFRAYKISKRFDDDISAVCAAFNLELDGGVVAEIRI 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763177138 399 GFGGVAATPETCPTLERALIGKQWQSADCLHLGKQMLKDaFNPIDDVRASAAYRNQVLSNLWHRFWLE 466
Cdd:TIGR02963 400 AFGGMAATPKRAAATEAALLGKPWNEATVEAAMAALAGD-FTPLSDMRASAEYRLLTAKNLLRRFFLE 466
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
20-475 |
5.09e-87 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 290.45 E-value: 5.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 20 LTLLQFLREHRkLTGTKEGCAAGDCGACTIVLGEVNNDGSALHYRTVNSCITLMSAVHGKQLIAVEHLAD-EGTLHPVQQ 98
Cdd:PLN02906 2 QTLLEYLRDLG-LTGTKLGCGEGGCGACTVMVSHYDRKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGNrRDGLHPVQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 99 ALLDYHGSQCGFCTPGFVMSMFALYHNA-TAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQgeaADHFAKTASNTLA- 176
Cdd:PLN02906 81 ALASMHGSQCGFCTPGFIMSMYALLRSSkTPPTEEQIEECLAGNLCRCTGYRPILDAFRVFAK---TDDALYTGVSSLSl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 177 -----------KLKDIQDNAGTAIGSSG---------------------VIM------------------------PTSR 200
Cdd:PLN02906 158 qdgepicpstgKPCSCGSKTTSAAGTCKsdrfqpisyseidgswytekeLIFppelllrkltplkllgnggltwyrPTSL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 201 EELANAIQGYPAAPLVAGSTDFGlsITQQLKNVE--KVINLSAMDSLKKCTKTEQALIIGAGAPL-----------NDIA 267
Cdd:PLN02906 238 QHLLELKAEYPDAKLVVGNTEVG--IEMRFKNAQypVLISPTHVPELNAIKVKDDGLEIGAAVRLselqnlfrkvvKERP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 268 SPLLSAFPQLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRASLHL-DNGQQVRVIPLKGFFTGYRQTQLEK 346
Cdd:PLN02906 316 AHETSACKAFIEQLKWFAGTQIRNVASIGGNICTASPISDLNPLWMAAGATFVIiSCDGDIRSVPASDFFLGYRKVDLKP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 347 GEWISAIEIPLLSKDNNVAAYKISKRMEDDISAVCA---VFnLTLVDG--VVTSLQTGFGGVAATPETCPTLERALIGKQ 421
Cdd:PLN02906 396 DEILLSVFLPWTRPFEYVKEFKQAHRRDDDIAIVNAgmrVK-LEEKDGewIVSDASIAYGGVAPLSVSARKTEEFLIGKP 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 763177138 422 WQSADCLHLGKQMLKDAFNPIDDVRASAAYRNQVLSNLWHRFWLE-----KQAQNTIET 475
Cdd:PLN02906 475 WNKETLQDALKVLQKDILIKEDAPGGMVEFRKSLALSFFFKFFLWvshqlEADGSTIET 533
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
197-358 |
1.63e-52 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 174.65 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 197 PTSREELANAIQGYPAAPLVAGSTDFGLSITQQLKNVEKVINLSAMDSLKKCTKTEQALIIGAGAPLNDIASPLL-SAFP 275
Cdd:pfam00941 8 PASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPLLrEAYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 276 QLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRASLHLDNGQQVRVIPLKGFFTGYRQTQLEKGEWISAIEI 355
Cdd:pfam00941 88 ALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEGERTVPLEDFFLGYGKTALEPGELITAVII 167
|
...
gi 763177138 356 PLL 358
Cdd:pfam00941 168 PLP 170
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
22-160 |
1.82e-37 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 134.92 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 22 LLQFLREHRKLTGTKEGCAAGDCGACTIVLgevnnDGsalhyRTVNSCITLMSAVHGKQLIAVEHLADEGTLHPVQQALL 101
Cdd:NF041020 30 LVHFLRDDLGFTGTHVGCDTSTCGACTVIM-----NG-----KSVKSCTVLAVQADGAEITTIEGLSKDGKLHPIQEAFW 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 763177138 102 DYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQ 160
Cdd:NF041020 100 ENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKEASQ 158
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
366-466 |
1.81e-23 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 94.61 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 366 AYKISKRMEDDISAVCAVFNLTLVDGVVTSLQTGFGGVAATPETCPTLERALIGKQWQSADCLHLGKQMLKDAFNPIDDV 445
Cdd:smart01092 1 AYKKSRRRDGDIALVSAAVALTLDGGRVTEARIALGGVAPTPKRAAEAEAALVGKPLTDEALARAAAAALAQDFTPLSDM 80
|
90 100
....*....|....*....|.
gi 763177138 446 RASAAYRNQVLSNLWHRFWLE 466
Cdd:smart01092 81 RASAEYRRQLAANLLRRALLE 101
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
2-74 |
3.86e-05 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 42.00 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 2 IRFLINKDLIELDdARADLTLLQFLREHRKltGTKEGCAAGDCGACT--IVLGEVNNDGSALHY------RTVNSCITLM 73
Cdd:cd00207 1 VTINVPGSGVEVE-VPEGETLLDAAREAGI--DIPYSCRAGACGTCKveVVEGEVDQSDPSLLDeeeaegGYVLACQTRV 77
|
.
gi 763177138 74 S 74
Cdd:cd00207 78 T 78
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
2-477 |
0e+00 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 720.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 2 IRFLINKDLIELDDARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLGEVNNDGsaLHYRTVNSCITLMSAVHGKQL 81
Cdd:COG4630 1 IRFLLNGELVELSDVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVGELDDGG--LRYRAVNACILFLPQLDGKAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 82 IAVEHLAD-EGTLHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQ 160
Cdd:COG4630 79 VTVEGLAGpDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAARAMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 161 GEAADHFAKTASNTLAKLKDIQDNAGTAI--GSSGVIMPTSREELANAIQGYPAAPLVAGSTDFGLSITQQLKNVEKVIN 238
Cdd:COG4630 159 APAPDPFAADRAAVAAALRALADGETVELgaGGSRFLAPATLDELAALLAAHPDARLVAGATDVGLWVTKQLRDLPPVIF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 239 LSAMDSLKKCTKTEQALIIGAGAPLNDIASPLLSAFPQLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRAS 318
Cdd:COG4630 239 LGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAHFPELAELLRRFASRQIRNAGTLGGNIANGSPIGDSPPALIALGAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 319 LHLDNGQQVRVIPLKGFFTGYRQTQLEKGEWISAIEIPLLSKDNNVAAYKISKRMEDDISAVCAVFNLTLVDGVVTSLQT 398
Cdd:COG4630 319 LVLRSGDGRRTLPLEDFFLGYRKTDLQPGEFVEAIRIPLPAAGQRLRAYKVSKRFDDDISAVCAAFALTLDDGTVTEARI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763177138 399 GFGGVAATPETCPTLERALIGKQWqSADCLHLGKQMLKDAFNPIDDVRASAAYRNQVLSNLWHRFWLEKQAQNTiETRV 477
Cdd:COG4630 399 AFGGMAATPKRARAAEAALLGQPW-TEATVAAAAAALAQDFTPLSDMRASAEYRLAVAANLLRRFFLETQGEAP-ATRV 475
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
2-466 |
0e+00 |
|
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 274365 [Multi-domain] Cd Length: 467 Bit Score: 580.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 2 IRFLINKDLIELDDARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLGEVNNDGSaLHYRTVNSCITLMSAVHGKQL 81
Cdd:TIGR02963 1 IRFFLNGETVTLSDVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVGELVDGGK-LRYRSVNACIQFLPSLDGKAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 82 IAVEHLAD-EGTLHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQ 160
Cdd:TIGR02963 80 VTVEDLRQpDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPILDAAEAAFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 161 GEAADHFAKTASNTLAKLKDIQDNAGTAIGSSG--VIMPTSREELANAIQGYPAAPLVAGSTDFGLSITQQLKNVEKVIN 238
Cdd:TIGR02963 160 YPCSDPLDADRAPIIERLRALRAGETVELNFGGerFIAPTTLDDLAALKAAHPDARIVAGSTDVGLWVTKQMRDLPDVIY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 239 LSAMDSLKKCTKTEQALIIGAGAPLNDIASPLLSAFPQLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRAS 318
Cdd:TIGR02963 240 VGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPELGELLRRFASLQIRNAGTLGGNIANGSPIGDSPPALIALGAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 319 LHLDNGQQVRVIPLKGFFTGYRQTQLEKGEWISAIEIPLLSKDNNVAAYKISKRMEDDISAVCAVFNLTLVDGVVTSLQT 398
Cdd:TIGR02963 320 LTLRKGEGRRTLPLEDFFIDYGKTDRQPGEFVEALHVPRPTPGERFRAYKISKRFDDDISAVCAAFNLELDGGVVAEIRI 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763177138 399 GFGGVAATPETCPTLERALIGKQWQSADCLHLGKQMLKDaFNPIDDVRASAAYRNQVLSNLWHRFWLE 466
Cdd:TIGR02963 400 AFGGMAATPKRAAATEAALLGKPWNEATVEAAMAALAGD-FTPLSDMRASAEYRLLTAKNLLRRFFLE 466
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
20-475 |
5.09e-87 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 290.45 E-value: 5.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 20 LTLLQFLREHRkLTGTKEGCAAGDCGACTIVLGEVNNDGSALHYRTVNSCITLMSAVHGKQLIAVEHLAD-EGTLHPVQQ 98
Cdd:PLN02906 2 QTLLEYLRDLG-LTGTKLGCGEGGCGACTVMVSHYDRKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGNrRDGLHPVQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 99 ALLDYHGSQCGFCTPGFVMSMFALYHNA-TAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQgeaADHFAKTASNTLA- 176
Cdd:PLN02906 81 ALASMHGSQCGFCTPGFIMSMYALLRSSkTPPTEEQIEECLAGNLCRCTGYRPILDAFRVFAK---TDDALYTGVSSLSl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 177 -----------KLKDIQDNAGTAIGSSG---------------------VIM------------------------PTSR 200
Cdd:PLN02906 158 qdgepicpstgKPCSCGSKTTSAAGTCKsdrfqpisyseidgswytekeLIFppelllrkltplkllgnggltwyrPTSL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 201 EELANAIQGYPAAPLVAGSTDFGlsITQQLKNVE--KVINLSAMDSLKKCTKTEQALIIGAGAPL-----------NDIA 267
Cdd:PLN02906 238 QHLLELKAEYPDAKLVVGNTEVG--IEMRFKNAQypVLISPTHVPELNAIKVKDDGLEIGAAVRLselqnlfrkvvKERP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 268 SPLLSAFPQLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRASLHL-DNGQQVRVIPLKGFFTGYRQTQLEK 346
Cdd:PLN02906 316 AHETSACKAFIEQLKWFAGTQIRNVASIGGNICTASPISDLNPLWMAAGATFVIiSCDGDIRSVPASDFFLGYRKVDLKP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 347 GEWISAIEIPLLSKDNNVAAYKISKRMEDDISAVCA---VFnLTLVDG--VVTSLQTGFGGVAATPETCPTLERALIGKQ 421
Cdd:PLN02906 396 DEILLSVFLPWTRPFEYVKEFKQAHRRDDDIAIVNAgmrVK-LEEKDGewIVSDASIAYGGVAPLSVSARKTEEFLIGKP 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 763177138 422 WQSADCLHLGKQMLKDAFNPIDDVRASAAYRNQVLSNLWHRFWLE-----KQAQNTIET 475
Cdd:PLN02906 475 WNKETLQDALKVLQKDILIKEDAPGGMVEFRKSLALSFFFKFFLWvshqlEADGSTIET 533
|
|
| CutB |
COG1319 |
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion] ... |
194-459 |
1.48e-64 |
|
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440930 [Multi-domain] Cd Length: 285 Bit Score: 210.36 E-value: 1.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 194 VIMPTSREELANAIQGY-PAAPLVAGSTDFGLSITQQLKNVEKVINLSAMDSLKKCTKTEQALIIGAGAPLNDIA-SPLL 271
Cdd:COG1319 6 YHRPTSLEEALALLAEHgPDARVLAGGTDLLPLMKLRLARPEHLVDINRIPELRGIEEEGGGLRIGALVTHAELAaSPLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 272 -SAFPQLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRASLHLDNGQQVRVIPLKGFFTGYRQTQLEKGEWI 350
Cdd:COG1319 86 rERYPLLAEAARAIASPQIRNRGTIGGNLANADPAADLPPALLALDATVELAGPDGERTIPAADFFLGPGETALEPGELI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 351 SAIEIPLLSKDNNVAAYKISKRMEDDISAVCAVFNLTLVDGVVTSLQTGFGGVAATPETCPTLERALIGKQWQSADCLHL 430
Cdd:COG1319 166 TAVRLPAPPAGAGSAYLKVGRRASDAIALVSVAVALRLDGGTIRDARIALGGVAPTPWRAREAEAALAGKPLSEEAIEAA 245
|
250 260
....*....|....*....|....*....
gi 763177138 431 GKQMLKDAfNPIDDVRASAAYRNQVLSNL 459
Cdd:COG1319 246 AEAAAAAA-DPIDDVRASAEYRRHLARVL 273
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
1-157 |
1.03e-61 |
|
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441683 [Multi-domain] Cd Length: 155 Bit Score: 198.39 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 1 MIRFLINKDLIELDdARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLgevnnDGsalhyRTVNSCITLMSAVHGKQ 80
Cdd:COG2080 3 MITLTVNGKPVEVD-VDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLV-----DG-----KAVRSCLTLAVQADGKE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 763177138 81 LIAVEHLADEGTLHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALA 157
Cdd:COG2080 72 ITTIEGLAEDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKR 148
|
|
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
4-422 |
2.87e-61 |
|
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase.
Pssm-ID: 132014 [Multi-domain] Cd Length: 1330 Bit Score: 216.80 E-value: 2.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 4 FLINKDLIELDDARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLGEVNNDGSALHYRTVNSCITLMSAVHGKQLIA 83
Cdd:TIGR02969 5 FYVNGRKVVEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPSTKSIRHHPVNACLTPICSLYGAAVTT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 84 VEHLADEGT-LHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQGE 162
Cdd:TIGR02969 85 VEGIGSTRTrLHPVQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 163 AA---------------------DHFAKTASN--------------------TLAKLKDIQDNAGTAIGSSGV--IMPTS 199
Cdd:TIGR02969 165 GCcqskengvccldqginglpefEEGDETSPElfseeeflpldptqelifppELMRMAEKQPQRTRVFYSERMmwISPVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 200 REELANAIQGYPAAPLVAGSTDFGLSItqQLKNV--EKVINLSAMDSLKKCTKTEQALIIGAG---APLNDIASPLLSAF 274
Cdd:TIGR02969 245 LKELLEAKFKYPQAPVVMGNTSVGPEV--KFKGVfhPVIISPDRIEELSVVNHTGDGLTLGAGlslAQVKDILADVVQKL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 275 PQ--------LAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRASLHLDNGQQVRVIPL-KGFFTGYRQTQLE 345
Cdd:TIGR02969 323 PEettqtyraLLKHLGTLAGSQIRNMASLGGHIISRHLDSDLNPLLAVGNCTLNLLSKEGKRQIPLsEQFLSKCPDADLK 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763177138 346 KGEWISAIEIPLLSKDNNVAAYKISKRMEDDISAVCAVFNLTLV--DGVVTSLQTGFGGVAATPETCPTLERALIGKQW 422
Cdd:TIGR02969 403 PQEILVSVNIPYSRKWEFVSAFRQAQRQQNALAIVNSGMRVFFGegDGIIRELSISYGGVGPTTICAKNSCQKLIGRPW 481
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
197-358 |
1.63e-52 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 174.65 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 197 PTSREELANAIQGYPAAPLVAGSTDFGLSITQQLKNVEKVINLSAMDSLKKCTKTEQALIIGAGAPLNDIASPLL-SAFP 275
Cdd:pfam00941 8 PASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPLLrEAYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 276 QLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRASLHLDNGQQVRVIPLKGFFTGYRQTQLEKGEWISAIEI 355
Cdd:pfam00941 88 ALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEGERTVPLEDFFLGYGKTALEPGELITAVII 167
|
...
gi 763177138 356 PLL 358
Cdd:pfam00941 168 PLP 170
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
4-356 |
1.19e-44 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 167.97 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 4 FLINKDLIELDDARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLGEVNNDGSALHYRTVNSCITLMSAVHGKQLIA 83
Cdd:PLN00192 8 FAVNGERFELSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLLSKYDPVLDQVEDFTVSSCLTLLCSVNGCSITT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 84 VEHLAD-EGTLHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRD------------DVLHALSGNLCRCTGYRP 150
Cdd:PLN00192 88 SEGLGNsKDGFHPIHKRFAGFHASQCGFCTPGMCISLFSALVNADKTDRPeppsgfskltvvEAEKAVSGNLCRCTGYRP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 151 IIEAalasCQGEAAD---------HFAKTASNTLAKL--------------------KDIQDNAGTAIGSSGVIMPTSRE 201
Cdd:PLN00192 168 IVDA----CKSFAADvdiedlglnSFWKKGESEEAKLsklppynhsdhictfpeflkKEIKSSLLLDSSRYRWYTPVSVE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 202 ELANAIQ----GYPAAPLVAGSTdfGLSITQQLKNVEKVINLSAMDSLKKCTKTEQALIIGAGAPLNDIASPLLS----- 272
Cdd:PLN00192 244 ELQSLLEsnnfDGVSVKLVVGNT--GTGYYKDEELYDKYIDIRHIPELSMIRRDEKGIEIGAVVTISKAIEALREeskse 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 273 -AFPQLAELITRFASLPIRNQATLGGNIANAS----PiGDMPPALLALRASLHLDNGQQVRVIPLKGFFtgyRQTQLEKG 347
Cdd:PLN00192 322 yVFKKIADHMEKIASRFVRNTGSIGGNLVMAQrkqfP-SDIATILLAAGSTVNIQNASKREKLTLEEFL---ERPPLDSK 397
|
....*....
gi 763177138 348 EWISAIEIP 356
Cdd:PLN00192 398 SLLLSVEIP 406
|
|
| 4hydroxCoAred |
TIGR03193 |
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ... |
14-158 |
1.77e-37 |
|
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts 4-hydroxybenzoyl-CoA to benzoyl-CoA, a common intermediate in the degradation of aromatic compounds. This protein family represents the gamma chain of this three-subunit enzyme.
Pssm-ID: 132237 [Multi-domain] Cd Length: 148 Bit Score: 134.23 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 14 DDARAD-LTLLQFLREHRKLTGTKEGCAAGDCGACTIVLgevnnDGsalhyRTVNSCITLMSAVHGKQLIAVEHLADEGT 92
Cdd:TIGR03193 12 EDAVADnMLLVDYLRDTVGLTGTKQGCDGGECGACTVLV-----DG-----RPRLACSTLAHRVAGRKVETVEGLATNGR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 763177138 93 LHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALAS 158
Cdd:TIGR03193 82 LSRLQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRAALAGNLCRCTGYVKIIESVEAA 147
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
22-160 |
1.82e-37 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 134.92 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 22 LLQFLREHRKLTGTKEGCAAGDCGACTIVLgevnnDGsalhyRTVNSCITLMSAVHGKQLIAVEHLADEGTLHPVQQALL 101
Cdd:NF041020 30 LVHFLRDDLGFTGTHVGCDTSTCGACTVIM-----NG-----KSVKSCTVLAVQADGAEITTIEGLSKDGKLHPIQEAFW 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 763177138 102 DYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQ 160
Cdd:NF041020 100 ENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKEASQ 158
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
84-155 |
1.37e-34 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 124.08 E-value: 1.37e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763177138 84 VEHLADEGTlHPVQQALLDYHGSQCGFCTPGFVMSMFALY-HNATAPTRDDVLHALSGNLCRCTGYRPIIEAA 155
Cdd:pfam01799 2 IEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLeRNPPPPTEAEIREALSGNLCRCTGYRRIVDAV 73
|
|
| PRK09908 |
PRK09908 |
xanthine dehydrogenase iron sulfur-binding subunit XdhC; |
20-162 |
1.74e-32 |
|
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
Pssm-ID: 182139 [Multi-domain] Cd Length: 159 Bit Score: 121.18 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 20 LTLLQFLREHrKLTGTKEGCAAGDCGACTIVLgevnnDGSAlhyrtVNSCITLMSAVHGKQLIAVEHLADEGTLHPVQQA 99
Cdd:PRK09908 26 TPLSELLREQ-GLLSVKQGCCVGECGACTVLV-----DGTA-----IDSCLYLAAWAEGKEIRTLEGEAKGGKLSHVQQA 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 763177138 100 LLDYHGSQCGFCTPGFVMSMFALYHNATAP--TRDDVLHALSGNLCRCTGYRPIIEAALASCQGE 162
Cdd:PRK09908 95 YAKSGAVQCGFCTPGLIMATTAMLAKPREKplTITEIRRGLAGNLCRCTGYQMIVNTVLDCEKTK 159
|
|
| pucE |
TIGR03198 |
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ... |
3-161 |
2.06e-32 |
|
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.
Pssm-ID: 132242 [Multi-domain] Cd Length: 151 Bit Score: 120.73 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 3 RFLINKDLIELDdARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLgevnnDGSAlhyrtVNSCITLMSAVHGKQLI 82
Cdd:TIGR03198 5 RFTVNGQAWEVA-AVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLI-----DGKL-----ANACLTMAYQADGHEIT 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763177138 83 AVEHLADEGtLHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEAALASCQG 161
Cdd:TIGR03198 74 TIEGIAENE-LDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGGIIRSACRIRRG 151
|
|
| PRK09971 |
PRK09971 |
xanthine dehydrogenase subunit XdhB; Provisional |
197-462 |
1.42e-31 |
|
xanthine dehydrogenase subunit XdhB; Provisional
Pssm-ID: 182175 [Multi-domain] Cd Length: 291 Bit Score: 122.84 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 197 PTSREELANAIQGYPAAPLVAGSTDFGLSITQQLKNVEKVINLSAMDSLKKCTKTEQ-ALIIGAGAPLNDIAS-PLLSA- 273
Cdd:PRK09971 10 AATLEEAIELLADNPQAKLIAGGTDVLIQLHHHNDRYRHLVSIHNIAELRGITLAEDgSIRIGAATTFTQIIEdPIIQKh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 274 FPQLAELITRFASLPIRNQATLGGNIANASPIGDMPPALLALRASLHLDNGQQVRVIPLKGFFTGYRQTQLEKGEWISAI 353
Cdd:PRK09971 90 LPALAEAAVSIGGPQIRNVATIGGNICNGATSADSAPPLFALDAKLEIHSPNGVRFVPINGFYTGPGKVSLEHDEILVAF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 354 EIPLLSKDNNVAAY-KISKRMEDDISAV-CAVfNLTLVDGVVTSLQTGFGGVAATPETCPTLERALIGKQWQSADCLHLG 431
Cdd:PRK09971 170 IIPPEPYEHAGGAYiKYAMRDAMDIATIgCAV-LCRLDNGNFEDLRLAFGVAAPTPIRCQHAEQTAKGAPLNLETLEAIG 248
|
250 260 270
....*....|....*....|....*....|.
gi 763177138 432 KQMLKDAfNPIDDVRASAAYRNQVLSNLWHR 462
Cdd:PRK09971 249 ELVLQDV-APRSSWRASKEFRLHLIQELTKR 278
|
|
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
4-154 |
2.90e-29 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 114.48 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 4 FLINKDLIELD-DARAdlTLLQFLREHRKLTGTKEGCAAGDCGACTIVLgevnnDGsalhyRTVNSCITLMSAVHGKQLI 82
Cdd:PRK11433 54 LKVNGKTEQLEvDTRT--TLLDALREHLHLTGTKKGCDHGQCGACTVLV-----NG-----RRLNACLTLAVMHQGAEIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 83 AVEHLADEGTLHPVQQALLDYHGSQCGFCTPGFVMSMFALYH------------NATAPTR---DDVLHALSGNLCRCTG 147
Cdd:PRK11433 122 TIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKeikdgipshvtvDLTAAPEltaDEIRERMSGNICRCGA 201
|
....*..
gi 763177138 148 YRPIIEA 154
Cdd:PRK11433 202 YSNILEA 208
|
|
| Se_dep_XDH |
TIGR03311 |
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional ... |
15-154 |
4.03e-29 |
|
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional xanthine dehydrogenase enzymes, which depend on molybdenum cofactor - molybdopterin bound to molybdate with two sulfur atoms as ligands. But all members of this family occur in species that contain markers for the biosynthesis of enzymes with a selenium-containing form of molybdenum cofactor. The member of this family from Enterococcus faecalis has been shown to act as a xanthine dehydrogenenase, and its activity if dependent on SelD (selenophosphate synthase), selenium, and molybdenum. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132354 [Multi-domain] Cd Length: 848 Bit Score: 121.49 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 15 DARADLTLLQFLREHRKLTGTKEGCAAGDCGACTIVLgevnnDGSAlhyrtVNSCITLMSAVHGKQLIAVEHLAdegtlh 94
Cdd:TIGR03311 11 DVNEEKKLLEFLREDLRLTGVKNGCGEGACGACTVIV-----NGKA-----VRACRFTTAKLAGKEITTVEGLT------ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 763177138 95 PVQQALLDYHGS-----QCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRCTGYRPIIEA 154
Cdd:TIGR03311 75 EREKDVYAWAFAkagavQCGFCIPGMVISAKALLDKNPNPTEAEIKKALKGNICRCTGYVKIIKA 139
|
|
| CO_deh_flav_C |
pfam03450 |
CO dehydrogenase flavoprotein C-terminal domain; |
365-466 |
2.13e-24 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 460921 [Multi-domain] Cd Length: 102 Bit Score: 97.25 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 365 AAYKISKRMEDDISAVCAVFNLTLVDGVVTSLQTGFGGVAATPETCPTLERALIGKQWQSADCLHLGKQMLKDaFNPIDD 444
Cdd:pfam03450 1 AAYKQAKRRDDDIAIVNAAFRVRLDGGTVEDARIAFGGVAPTPIRATEAEAALIGKPWDEETLEAAAALLLED-LSPLSD 79
|
90 100
....*....|....*....|..
gi 763177138 445 VRASAAYRNQVLSNLWHRFWLE 466
Cdd:pfam03450 80 PRGSAEYRRHLARSLLFRFLLE 101
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
366-466 |
1.81e-23 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 94.61 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 366 AYKISKRMEDDISAVCAVFNLTLVDGVVTSLQTGFGGVAATPETCPTLERALIGKQWQSADCLHLGKQMLKDAFNPIDDV 445
Cdd:smart01092 1 AYKKSRRRDGDIALVSAAVALTLDGGRVTEARIALGGVAPTPKRAAEAEAALVGKPLTDEALARAAAAALAQDFTPLSDM 80
|
90 100
....*....|....*....|.
gi 763177138 446 RASAAYRNQVLSNLWHRFWLE 466
Cdd:smart01092 81 RASAEYRRQLAANLLRRALLE 101
|
|
| PRK09800 |
PRK09800 |
putative hypoxanthine oxidase; Provisional |
66-158 |
1.96e-06 |
|
putative hypoxanthine oxidase; Provisional
Pssm-ID: 182084 [Multi-domain] Cd Length: 956 Bit Score: 50.60 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 66 VNSCITLMSAVHGKQLIAVEHLADEGTLHPVQQALLDYHGSQCGFCTPGFVMSMFALYHNATAPTRDDVLHALSGNLCRC 145
Cdd:PRK09800 56 VNASLLIAAQLEKADIRTAESLGKWNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRD 135
|
90
....*....|....
gi 763177138 146 TGYRPIIEA-ALAS 158
Cdd:PRK09800 136 AGWQQYYQViELAV 149
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
2-74 |
3.86e-05 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 42.00 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 2 IRFLINKDLIELDdARADLTLLQFLREHRKltGTKEGCAAGDCGACT--IVLGEVNNDGSALHY------RTVNSCITLM 73
Cdd:cd00207 1 VTINVPGSGVEVE-VPEGETLLDAAREAGI--DIPYSCRAGACGTCKveVVEGEVDQSDPSLLDeeeaegGYVLACQTRV 77
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.
gi 763177138 74 S 74
Cdd:cd00207 78 T 78
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| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
192-330 |
2.32e-03 |
|
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 426326 [Multi-domain] Cd Length: 139 Bit Score: 38.34 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177138 192 SGVIMPTSREELANAIQ-----GYPAAPLVAGSTDFGLSITQQlknvEKVINLSAMDSLKKCTKTEQALIIGAGAPLNDi 266
Cdd:pfam01565 2 AAVVLPESEEEVAAIVRlanenGLPVLPRGGGSSLLGGAVQTG----GIVLDLSRLNGILEIDPEDGTATVEAGVTLGD- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 763177138 267 asplLSAFPQLAELITR--FASLPirnQATLGGNIANASpigdmpPALLALRASLHLDNGQQVRVI 330
Cdd:pfam01565 77 ----LVRALAAKGLLLGldPGSGI---PGTVGGAIATNA------GGYGSEKYGLTRDNVLGLEVV 129
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