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Conserved domains on  [gi|2735078528|ref|WP_346744370|]
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tRNA dihydrouridine synthase DusB [uncultured Streptococcus sp.]

Protein Classification

tRNA dihydrouridine synthase( domain architecture ID 11414563)

tRNA dihydrouridine synthase catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs

CATH:  3.20.20.70|1.10.1200.80
EC:  1.3.1.-
Gene Ontology:  GO:0017150|GO:0008033|GO:0050660|GO:0016491
PubMed:  30149704|34798057
SCOP:  4000080

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 11-321 7.25e-150

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 423.35  E-value: 7.25e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  11 GNVEIPNRTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARAA 90
Cdd:COG0042     1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  91 EFIQENtKTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSL-AVENALAAEAAG 169
Cdd:COG0042    81 RIAEEL-GADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDEnALEFARIAEDAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 170 VSALAMHGRTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINHYF 249
Cdd:COG0042   160 AAALTVHGRTREQRYKGPADWDAIARVKEAV-SIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYL 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735078528 250 ETGEIlPDLTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLRGTSGAAKLRGAISQANTLAEIEELL 321
Cdd:COG0042   239 AGGEA-PPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELL 309
 
Name Accession Description Interval E-value
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 11-321 7.25e-150

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 423.35  E-value: 7.25e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  11 GNVEIPNRTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARAA 90
Cdd:COG0042     1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  91 EFIQENtKTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSL-AVENALAAEAAG 169
Cdd:COG0042    81 RIAEEL-GADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDEnALEFARIAEDAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 170 VSALAMHGRTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINHYF 249
Cdd:COG0042   160 AAALTVHGRTREQRYKGPADWDAIARVKEAV-SIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYL 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735078528 250 ETGEIlPDLTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLRGTSGAAKLRGAISQANTLAEIEELL 321
Cdd:COG0042   239 AGGEA-PPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELL 309
nifR3_yhdG TIGR00737
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ...
 10-321 2.49e-130

putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General]


Pssm-ID: 129820  Cd Length: 319  Bit Score: 374.39  E-value: 2.49e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  10 IGNVEIPNRTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARA 89
Cdd:TIGR00737   1 IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLFGSDPDTMAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  90 AEfIQENTKTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSL-AVENALAAEAA 168
Cdd:TIGR00737  81 AK-INEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRIGWDDAHInAVEAARIAEDA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 169 GVSALAMHGRTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINHY 248
Cdd:TIGR00737 160 GAQAVTLHGRTRAQGYSGEANWDIIARVKQAV-RIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEQY 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735078528 249 FETGEILPDLTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLRGTSGAAKLRGAISQANTLAEIEELL 321
Cdd:TIGR00737 239 LTTGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKHIAWYLKGFPGNAALRQTLNHASSFQEVKQLL 311
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 18-250 3.34e-111

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 322.14  E-value: 3.34e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  18 RTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARAAEFIQENt 97
Cdd:cd02801     1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLAEAAKIVEEL- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  98 KTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSLAVENALAAEAAGVSALAMHG 177
Cdd:cd02801    80 GADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGWDDEEETLELAKALEDAGASALTVHG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735078528 178 RTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINHYFE 250
Cdd:cd02801   160 RTREQRYSGPADWDYIAEIKEAV-SIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 20-322 2.75e-101

Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.


Pssm-ID: 426126  Cd Length: 309  Bit Score: 300.01  E-value: 2.75e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  20 VLAPMAGVTNSAFRTIAKELGAG-LVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARAAEFIQENtK 98
Cdd:pfam01207   1 LLAPMAGVTDLPFRRLVREYGAGdLVYTEMVTAKAQLRPEKVRIRMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDR-G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  99 TDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSL-AVENALAAEAAGVSALAMHG 177
Cdd:pfam01207  80 ADGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHEnAVEIAKIVEDAGAQALTVHG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 178 RTREQMYTGHADLETLHKVAQALTkIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQInHYFETGEILPD 257
Cdd:pfam01207 160 RTRAQNYEGTADWDAIKQVKQAVS-IPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAEQ-HTVKTGEFGPS 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735078528 258 LTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLRGTSGAAKLRGAISQANTLAEIEELLQ 322
Cdd:pfam01207 238 PPLAEEAEKVLRHLPYLEEFLGEDKGLRHARKHLAWYLKGFPGAAELRRELNDVFDPVEALINLD 302
PRK10415 PRK10415
tRNA-dihydrouridine synthase B; Provisional
 10-296 3.87e-76

tRNA-dihydrouridine synthase B; Provisional


Pssm-ID: 182440  Cd Length: 321  Bit Score: 236.41  E-value: 3.87e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  10 IGNVEIPNRTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKT-LHMLHIDEgENPVSIQLFGSDEDSLAR 88
Cdd:PRK10415    3 IGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSrLRMVHIDE-PGIRTVQIAGSDPKEMAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  89 AAEfIQENTKTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWS-DPSLAVENALAAEA 167
Cdd:PRK10415   82 AAR-INVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIRTGWApEHRNCVEIAQLAED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 168 AGVSALAMHGRTREQMYTGHADLETLHKVAQALTkIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINH 247
Cdd:PRK10415  161 CGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVS-IPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQH 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2735078528 248 YFETGEILPDLTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLR 296
Cdd:PRK10415  240 YLDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQ 288
 
Name Accession Description Interval E-value
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 11-321 7.25e-150

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 423.35  E-value: 7.25e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  11 GNVEIPNRTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARAA 90
Cdd:COG0042     1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  91 EFIQENtKTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSL-AVENALAAEAAG 169
Cdd:COG0042    81 RIAEEL-GADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDEnALEFARIAEDAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 170 VSALAMHGRTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINHYF 249
Cdd:COG0042   160 AAALTVHGRTREQRYKGPADWDAIARVKEAV-SIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYL 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735078528 250 ETGEIlPDLTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLRGTSGAAKLRGAISQANTLAEIEELL 321
Cdd:COG0042   239 AGGEA-PPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELL 309
nifR3_yhdG TIGR00737
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ...
 10-321 2.49e-130

putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General]


Pssm-ID: 129820  Cd Length: 319  Bit Score: 374.39  E-value: 2.49e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  10 IGNVEIPNRTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARA 89
Cdd:TIGR00737   1 IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLFGSDPDTMAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  90 AEfIQENTKTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSL-AVENALAAEAA 168
Cdd:TIGR00737  81 AK-INEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRIGWDDAHInAVEAARIAEDA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 169 GVSALAMHGRTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINHY 248
Cdd:TIGR00737 160 GAQAVTLHGRTRAQGYSGEANWDIIARVKQAV-RIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEQY 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735078528 249 FETGEILPDLTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLRGTSGAAKLRGAISQANTLAEIEELL 321
Cdd:TIGR00737 239 LTTGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKHIAWYLKGFPGNAALRQTLNHASSFQEVKQLL 311
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 18-250 3.34e-111

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 322.14  E-value: 3.34e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  18 RTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARAAEFIQENt 97
Cdd:cd02801     1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLAEAAKIVEEL- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  98 KTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSLAVENALAAEAAGVSALAMHG 177
Cdd:cd02801    80 GADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGWDDEEETLELAKALEDAGASALTVHG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735078528 178 RTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINHYFE 250
Cdd:cd02801   160 RTREQRYSGPADWDYIAEIKEAV-SIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 20-322 2.75e-101

Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.


Pssm-ID: 426126  Cd Length: 309  Bit Score: 300.01  E-value: 2.75e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  20 VLAPMAGVTNSAFRTIAKELGAG-LVVMEMVSDKGIQYNNEKTLHMLHIDEGENPVSIQLFGSDEDSLARAAEFIQENtK 98
Cdd:pfam01207   1 LLAPMAGVTDLPFRRLVREYGAGdLVYTEMVTAKAQLRPEKVRIRMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDR-G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  99 TDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWSDPSL-AVENALAAEAAGVSALAMHG 177
Cdd:pfam01207  80 ADGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHEnAVEIAKIVEDAGAQALTVHG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 178 RTREQMYTGHADLETLHKVAQALTkIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQInHYFETGEILPD 257
Cdd:pfam01207 160 RTRAQNYEGTADWDAIKQVKQAVS-IPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAEQ-HTVKTGEFGPS 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735078528 258 LTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLRGTSGAAKLRGAISQANTLAEIEELLQ 322
Cdd:pfam01207 238 PPLAEEAEKVLRHLPYLEEFLGEDKGLRHARKHLAWYLKGFPGAAELRRELNDVFDPVEALINLD 302
PRK10415 PRK10415
tRNA-dihydrouridine synthase B; Provisional
 10-296 3.87e-76

tRNA-dihydrouridine synthase B; Provisional


Pssm-ID: 182440  Cd Length: 321  Bit Score: 236.41  E-value: 3.87e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  10 IGNVEIPNRTVLAPMAGVTNSAFRTIAKELGAGLVVMEMVSDKGIQYNNEKT-LHMLHIDEgENPVSIQLFGSDEDSLAR 88
Cdd:PRK10415    3 IGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSrLRMVHIDE-PGIRTVQIAGSDPKEMAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  89 AAEfIQENTKTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWS-DPSLAVENALAAEA 167
Cdd:PRK10415   82 AAR-INVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIRTGWApEHRNCVEIAQLAED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 168 AGVSALAMHGRTREQMYTGHADLETLHKVAQALTkIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQINH 247
Cdd:PRK10415  161 CGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVS-IPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQH 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2735078528 248 YFETGEILPDLTFEDKMKIAYEHLKRLIDLKGEKIAVREFRGLAPHYLR 296
Cdd:PRK10415  240 YLDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQ 288
PRK10550 PRK10550
tRNA dihydrouridine(16) synthase DusC;
18-241 8.25e-30

tRNA dihydrouridine(16) synthase DusC;


Pssm-ID: 236713  Cd Length: 312  Bit Score: 115.29  E-value: 8.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  18 RTVLAPMAGVTNSAFRTIAKELGA-GLVVMEM--VSDKGIQ----YNNEKTLHMLHIDEGENPVSIQLFGSDEDSLA--- 87
Cdd:PRK10550    2 RVLLAPMEGVLDSLVRELLTEVNDyDLCITEFlrVVDQLLPvkvfHRLCPELHNASRTPSGTLVRIQLLGQYPQWLAena 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  88 -RAAEFIQENtktdiVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVL--DIPLTVKMRTGWSDPSLAVENALA 164
Cdd:PRK10550   82 aRAVELGSWG-----VDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVTVKVRLGWDSGERKFEIADA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735078528 165 AEAAGVSALAMHGRTREQMYTG-HADLETLHKVAQALTkIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYL 241
Cdd:PRK10550  157 VQQAGATELVVHGRTKEDGYRAeHINWQAIGEIRQRLT-IPVIANGEIWDWQSAQQCMAITGCDAVMIGRGALNIPNL 233
PRK11815 PRK11815
tRNA dihydrouridine(20/20a) synthase DusA;
9-273 1.21e-25

tRNA dihydrouridine(20/20a) synthase DusA;


Pssm-ID: 236991 [Multi-domain]  Cd Length: 333  Bit Score: 104.45  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528   9 MIGNVEIPNRTV-LAPMAGVTNSAFRTIAKELGAG-LVVMEMVSDKGIQYNNEKTLhmLHIDEGENPVSIQLFGSDEDSL 86
Cdd:PRK11815    2 PEKMSKLPSRRFsVAPMMDWTDRHCRYFHRLLSRHaLLYTEMVTTGAIIHGDRERL--LAFDPEEHPVALQLGGSDPADL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  87 ARAAEfIQENTKTDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMRTGWS--DPSLAVEN-AL 163
Cdd:PRK11815   80 AEAAK-LAEDWGYDEINLNVGCPSDRVQNGRFGACLMAEPELVADCVKAMKDAVSIPVTVKHRIGIDdqDSYEFLCDfVD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 164 AAEAAGVSALAMHGRTreqmytghADLETL------------HKVAQALTK----IPFIANGDIRTVQDAKQRIEEVgaD 227
Cdd:PRK11815  159 TVAEAGCDTFIVHARK--------AWLKGLspkenreippldYDRVYRLKRdfphLTIEINGGIKTLEEAKEHLQHV--D 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2735078528 228 AVMIGRAAMGNPYLFNQINHYFeTGEILPDLTFED---KMkIAY--EHLKR 273
Cdd:PRK11815  229 GVMIGRAAYHNPYLLAEVDREL-FGEPAPPLSRSEvleAM-LPYieRHLAQ 277
arch_FMN cd02911
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ...
 18-235 3.79e-14

Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent flavin oxidoreductase (oxidored) FMN-binding family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN. The specific function of this group is unknown.


Pssm-ID: 239237 [Multi-domain]  Cd Length: 233  Bit Score: 70.82  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  18 RTVLAPMAGVTNSAFRTIAKELgAGLVVM----------------------EMVSDKGIQYNNEKtlhMLHIDEGENPVS 75
Cdd:cd02911     1 PVALASMAGITDGDFCRKRADH-AGLVFLggynldertieaarklvkrgrkEFLPDDPLEFIEGE---IKALKDSNVLVG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  76 IQLFGSDEDSLARAAEFIQENTktDIVDINMGCPVNKIVKNEAGAMWLKDPDKIYSIINKVQSvLDIPLTVKMRTGWSDP 155
Cdd:cd02911    77 VNVRSSSLEPLLNAAALVAKNA--AILEINAHCRQPEMVEAGAGEALLKDPERLSEFIKALKE-TGVPVSVKIRAGVDVD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 156 SLAVENALaaEAAGvsALAMHgrtREQMYTG-HADLETLHKVAQALTkipFIANGDIRTVQDAKQRIEEvGADAVMIGRA 234
Cdd:cd02911   154 DEELARLI--EKAG--ADIIH---VDAMDPGnHADLKKIRDISTELF---IIGNNSVTTIESAKEMFSY-GADMVSVARA 222


                  .
gi 2735078528 235 A 235
Cdd:cd02911   223 S 223
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 67-245 7.37e-13

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091 [Multi-domain]  Cd Length: 296  Bit Score: 67.96  E-value: 7.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  67 IDEGENPVSIQLFGSDEDSLARAAEFIQEnTKTDIVDINMGCPvNkiVKnEAGAMWLKDPDKIYSIINKVQSVLDIPLTV 146
Cdd:cd04740    85 LREFGTPVIASIAGSTVEEFVEVAEKLAD-AGADAIELNISCP-N--VK-GGGMAFGTDPEAVAEIVKAVKKATDVPVIV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 147 KMrTGWSDPslAVENALAAEAAGVSALAM------------HGRTREQMYTGH---------AdLETLHKVAQAlTKIPF 205
Cdd:cd04740   160 KL-TPNVTD--IVEIARAAEEAGADGLTLintlkgmaidieTRKPILGNVTGGlsgpaikpiA-LRMVYQVYKA-VEIPI 234

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2735078528 206 IANGDIRTVQDAkqrIE--EVGADAVMIGRAAMGNPYLFNQI 245
Cdd:cd04740   235 IGVGGIASGEDA---LEflMAGASAVQVGTANFVDPEAFKEI 273
PRK07259 PRK07259
dihydroorotate dehydrogenase;
74-247 2.09e-11

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 63.63  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  74 VSIqlFGSDEDSLARAAEFIQENTKTDIVDINMGCPvNkiVKnEAGAMWLKDPDKIYSIINKVQSVLDIPLTVKMrtgws 153
Cdd:PRK07259   96 ANV--AGSTEEEYAEVAEKLSKAPNVDAIELNISCP-N--VK-HGGMAFGTDPELAYEVVKAVKEVVKVPVIVKL----- 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 154 DPSLA--VENALAAEAAGVSAL-------AMhgrtREQMYTGHADLET-----------------LHKVAQAlTKIPFIA 207
Cdd:PRK07259  165 TPNVTdiVEIAKAAEEAGADGLslintlkGM----AIDIKTRKPILANvtgglsgpaikpialrmVYQVYQA-VDIPIIG 239

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2735078528 208 NGDIRTVQDAkqrIEEV--GADAVMIGRAAMGNPYLFNQINH 247
Cdd:PRK07259  240 MGGISSAEDA---IEFImaGASAVQVGTANFYDPYAFPKIIE 278
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 71-246 3.17e-11

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 63.14  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  71 ENPVSIQLFGSDEDSLARAAEFIQEnTKTDIVDINMGCPvnkivkNEAGAMWL-KDPDKIYSIINKVQSVLDIPLTVKMr 149
Cdd:cd02810    98 GQPLIASVGGSSKEDYVELARKIER-AGAKALELNLSCP------NVGGGRQLgQDPEAVANLLKAVKAAVDIPLLVKL- 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 150 TGWSDPSLAVENALAAEAAGVSALAMHGRT-------------REQMYTG-------HADLETLHKVAQAL-TKIPFIAN 208
Cdd:cd02810   170 SPYFDLEDIVELAKAAERAGADGLTAINTIsgrvvdlktvgpgPKRGTGGlsgapirPLALRWVARLAARLqLDIPIIGV 249

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2735078528 209 GDIRTVQDAKQRIeEVGADAVMIGRAAMGN-PYLFNQIN 246
Cdd:cd02810   250 GGIDSGEDVLEML-MAGASAVQVATALMWDgPDVIRKIK 287
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 74-246 1.19e-10

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 61.24  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  74 VSIqlFGSDEDSLARAAEFIQEnTKTDIVDINMGCPvNkiVKNEaGAMWLKDPDKIYSIINKVQSVLDIPLTVKMrtgws 153
Cdd:COG0167    97 VNI--GGNTVEDYVELARRLAD-AGADYLELNISCP-N--TPGG-GRALGQDPEALAELLAAVKAATDKPVLVKL----- 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 154 DPSLA--VENALAAEAAGVSALAM------------HGRTREQMYTG---------HAdLETLHKVAQAL-TKIPFIANG 209
Cdd:COG0167   165 APDLTdiVEIARAAEEAGADGVIAinttlgraidleTRRPVLANEAGglsgpalkpIA-LRMVREVAQAVgGDIPIIGVG 243

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2735078528 210 DIRTVQDAKQRIeEVGADAVMIGRAAMGN-PYLFNQIN 246
Cdd:COG0167   244 GISTAEDALEFI-LAGASAVQVGTALFYEgPGLVRRII 280
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 6-243 3.64e-10

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 60.28  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528   6 TPFMIGNVEIPNRTVLAPMagVTNSA-------------FRTIAKElGAGLVVME--MVSDKGIQYNNEKTLH------- 63
Cdd:cd02803     2 SPIKIGGLTLKNRIVMAPM--TENMAtedgtptdelieyYEERAKG-GVGLIITEaaYVDPEGKGYPGQLGIYddeqipg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  64 ------MLHidEGENPVSIQL----------------FGSDEDSLARAAEFIQENTKTDIVDInmgcpVNKIVK-----N 116
Cdd:cd02803    79 lrklteAVH--AHGAKIFAQLahagrqaqpnltggppPAPSAIPSPGGGEPPREMTKEEIEQI-----IEDFAAaarraK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 117 EAG-------------------AMWLKDPDK-----------IYSIINKVQSVL--DIPLTVKM-----RTGWSDPSLAV 159
Cdd:cd02803   152 EAGfdgveihgahgyllsqflsPYTNKRTDEyggslenrarfLLEIVAAVREAVgpDFPVGVRLsaddfVPGGLTLEEAI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 160 ENALAAEAAGVSALAMHGRTREQMYTGHAD--------LETLHKVAQALtKIPFIANGDIRTVQDAKQRIEEVGADAVMI 231
Cdd:cd02803   232 EIAKALEEAGVDALHVSGGSYESPPPIIPPpyvpegyfLELAEKIKKAV-KIPVIAVGGIRDPEVAEEILAEGKADLVAL 310

                         330
                  ....*....|..
gi 2735078528 232 GRAAMGNPYLFN 243
Cdd:cd02803   311 GRALLADPDLPN 322
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 1-245 1.54e-08

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 55.18  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528   1 MTNLNTPFMIGNVEIPNRTVLAPMAgvTNSA-------------FRTIAKElGAGLVVME--MVSDKGIQYNNEKTLH-- 63
Cdd:COG1902     4 MPKLFSPLTLGGLTLKNRIVMAPMT--RGRAdedgvptdlhaayYAQRARG-GAGLIITEatAVSPEGRGYPGQPGIWdd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  64 -----------------------MLH--------IDEGENPVS---IQLFG--------SDED------------SLARA 89
Cdd:COG1902    81 eqiaglrrvtdavhaaggkifiqLWHagrkahpdLPGGWPPVApsaIPAPGgpptpralTTEEieriiedfaaaaRRAKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  90 AEFiqentktDIVDINM----------------------GCPVNKI---------VKNEAGAmwlkdpdkiysiinkvqs 138
Cdd:COG1902   161 AGF-------DGVEIHGahgylldqflspltnqrtdeygGSLENRArfllevveaVRAAVGP------------------ 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 139 vlDIPLTVK------MRTGWsDPSLAVENALAAEAAGVSAL-----AMHGRTREQMYTGHADLETLHKVAQALTKIPFIA 207
Cdd:COG1902   216 --DFPVGVRlsptdfVEGGL-TLEESVELAKALEEAGVDYLhvssgGYEPDAMIPTIVPEGYQLPFAARIRKAVGIPVIA 292

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2735078528 208 NGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYLFNQI 245
Cdd:COG1902   293 VGGITTPEQAEAALASGDADLVALGRPLLADPDLPNKA 330
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 20-233 1.36e-05

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 45.27  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  20 VLAPMAGVTN---SAFRTIAKELGAGLVVMEMVSDKGIQYNNE-KTLHMLHIDEGENPVSIQLFGSDEDSLARAAEFIQE 95
Cdd:cd04722     2 ILALLAGGPSgdpVELAKAAAEAGADAIIVGTRSSDPEEAETDdKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAAAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  96 NTKTDIVDINMGCPVNkivkneagamwlkdPDKIYSIINKV-QSVLDIPLTVKMRTGWsdpslaVENALAAEAAGVSALA 174
Cdd:cd04722    82 AAGADGVEIHGAVGYL--------------AREDLELIRELrEAVPDVKVVVKLSPTG------ELAAAAAEEAGVDEVG 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735078528 175 MHGRTREQM---YTGHADLETlhKVAQALTKIPFIANGDIRTVQDAKQrIEEVGADAVMIGR 233
Cdd:cd04722   142 LGNGGGGGGgrdAVPIADLLL--ILAKRGSKVPVIAGGGINDPEDAAE-ALALGADGVIVGS 200
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
159-234 2.79e-05

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 44.37  E-value: 2.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735078528 159 VENALAAEAAGVSALA--MHGRTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIeEVGADAVMIGRA 234
Cdd:PRK01130  129 LEEGLAAQKLGFDFIGttLSGYTEETKKPEEPDFALLKELLKAV-GCPVIAEGRINTPEQAKKAL-ELGAHAVVVGGA 204
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 159-234 7.46e-05

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 43.33  E-value: 7.46e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735078528 159 VENALAAEAAGVSAL--AMHGRTREQMYTGHADLETLHKVAQALtKIPFIANGDIRTVQDAKQRIeEVGADAVMIGRA 234
Cdd:cd04729   133 LEEALNAAKLGFDIIgtTLSGYTEETAKTEDPDFELLKELRKAL-GIPVIAEGRINSPEQAAKAL-ELGADAVVVGSA 208
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 172-264 1.43e-04

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 42.97  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 172 ALAMHGRTREQMYTGHADLETLHKVAQAL-TKIPFIANGDIRTVQDAKQRIEEvGADAVMIGRAAMGNPYLF-------- 242
Cdd:cd04735   253 HISLWDFDRKSRRGRDDNQTIMELVKERIaGRLPLIAVGSINTPDDALEALET-GADLVAIGRGLLVDPDWVekikegre 331

                          90       100
                  ....*....|....*....|..
gi 2735078528 243 NQINHYFETgEILPDLTFEDKM 264
Cdd:cd04735   332 DEINLEIDP-DDLEELKIPPAL 352
FMN_dh pfam01070
FMN-dependent dehydrogenase;
157-236 4.33e-04

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 41.75  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 157 LAVENALAAEAAGVSA--LAMHG-RtreQMYTGHADLETLHKVAQAL-TKIPFIANGDIRTVQDakqrieeV------GA 226
Cdd:pfam01070 227 LSPEDAKRAVEAGVDGivVSNHGgR---QLDGAPATIDALPEIVAAVgGRIPVLVDGGIRRGTD-------VlkalalGA 296

                          90
                  ....*....|
gi 2735078528 227 DAVMIGRAAM 236
Cdd:pfam01070 297 DAVLLGRPFL 306
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 189-249 4.61e-04

Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439877  Cd Length: 251  Bit Score: 41.16  E-value: 4.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735078528 189 DLETLHKVAQALTkIPFIANGDIRTVQDAKQRIEEvGADAVMIGRAAMGNPYLFNQINHYF 249
Cdd:COG0107    61 MLDVVRRVAEEVF-IPLTVGGGIRSVEDARRLLRA-GADKVSINSAAVKNPELITEAAERF 119
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 154-249 5.54e-04

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 40.54  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 154 DPslaVENALAAEAAGVSAL-------AMHGRTReqmytghaDLETLHKVAQALTkIPFIANGDIRTVQDAKqRIEEVGA 226
Cdd:pfam00977  30 DP---VELAKRYEEEGADELhfvdldaAKEGRPV--------NLDVVEEIAEEVF-IPVQVGGGIRSLEDVE-RLLSAGA 96

                          90       100
                  ....*....|....*....|...
gi 2735078528 227 DAVMIGRAAMGNPYLFNQINHYF 249
Cdd:pfam00977  97 DRVIIGTAAVKNPELIKEAAEKF 119
PRK08255 PRK08255
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
6-49 1.14e-03

bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;


Pssm-ID: 236203 [Multi-domain]  Cd Length: 765  Bit Score: 40.69  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2735078528   6 TPFMIGNVEIPNRTVLAPMA------GVTNsAFRTI---AKEL-GAGLVVMEMV 49
Cdd:PRK08255  401 TPFRLRGLTLKNRVVVSPMAmysavdGVPG-DFHLVhlgARALgGAGLVMTEMT 453
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 189-234 1.30e-03

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 39.56  E-value: 1.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2735078528 189 DLETLHKVAqALTKIPFIANGDIRTVQDAKqRIEEVGADAVMIGRA 234
Cdd:cd04723   177 DLELLERLA-ARADIPVIAAGGVRSVEDLE-LLKKLGASGALVASA 220
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 160-233 1.53e-03

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 39.73  E-value: 1.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735078528 160 ENALAAEAAGVSALAMHGRTREQMYTGHADLETLHKVAQAL-TKIPFIANGDIRTVQDAKQRIEEvGADAVMIGR 233
Cdd:cd04737   233 EDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVnHRVPIIFDSGVRRGEHVFKALAS-GADAVAVGR 306
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 73-236 2.02e-03

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 39.35  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528  73 PVSIQ-LFGSD-EDSLARAAEfiqentKTDI---VDINMGCPVNKIVKNEAGAMW-----LKDPDKIYSIINKVQS---- 138
Cdd:cd02809    71 PTGLQgLAHPDgELATARAAA------AAGIpftLSTVSTTSLEEVAAAAPGPRWfqlyvPRDREITEDLLRRAEAagyk 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 139 --VLDIPLTV-----------KMRTGWSDP-----SLAVENALAAEAAGVSALAM---HGRtreQMYTGHADLETLHKVA 197
Cdd:cd02809   145 alVLTVDTPVlgrrltwddlaWLRSQWKGPlilkgILTPEDALRAVDAGADGIVVsnhGGR---QLDGAPATIDALPEIV 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2735078528 198 QAL-TKIPFIANGDIRTVQD-----AkqrieeVGADAVMIGRAAM 236
Cdd:cd02809   222 AAVgGRIEVLLDGGIRRGTDvlkalA------LGADAVLIGRPFL 260
OYE_YqiM_FMN cd02932
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ...
 201-241 2.13e-03

Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.


Pssm-ID: 239242 [Multi-domain]  Cd Length: 336  Bit Score: 39.40  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2735078528 201 TKIPFIANGDIRTVQDAKQRIEEVGADAVMIGRAAMGNPYL 241
Cdd:cd02932   289 AGIPVIAVGLITDPEQAEAILESGRADLVALGRELLRNPYW 329
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 189-249 2.61e-03

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273241  Cd Length: 254  Bit Score: 38.89  E-value: 2.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735078528 189 DLETLHKVAQALTkIPFIANGDIRTVQDAKqRIEEVGADAVMIGRAAMGNPYLFNQINHYF 249
Cdd:TIGR00735  62 MIDVVERTAETVF-IPLTVGGGIKSIEDVD-KLLRAGADKVSINTAAVKNPELIYELADRF 120
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 189-245 2.70e-03

The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240082  Cd Length: 243  Bit Score: 38.60  E-value: 2.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2735078528 189 DLETLHKVAQALTkIPFIANGDIRTVQDAKqRIEEVGADAVMIGRAAMGNPYLFNQI 245
Cdd:cd04731    59 MLDVVERVAEEVF-IPLTVGGGIRSLEDAR-RLLRAGADKVSINSAAVENPELIREI 113
OYE_YqiM_FMN cd02932
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ...
 4-48 6.03e-03

Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.


Pssm-ID: 239242 [Multi-domain]  Cd Length: 336  Bit Score: 37.86  E-value: 6.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528   4 LNTPFMIGNVEIPNRTVLAPMA------GVTNS---------AFRtiakelGAGLVVMEM 48
Cdd:cd02932     1 LFTPLTLRGVTLKNRIVVSPMCqysaedGVATDwhlvhygsrALG------GAGLVIVEA 54
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 4-104 6.66e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 37.96  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528   4 LNTPFMIGN-VEIPNRTVLAPMagVTNSAFR--TIAKEL---------GAGLVVME--MVSDKGIQYnnektlhmlhide 69
Cdd:cd04735     1 LFEPFTLKNgVTLKNRFVMAPM--TTYSSNPdgTITDDElayyqrragGVGMVITGatYVSPSGIGF------------- 65

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2735078528  70 gENPVSIQlfgSDED--SLARAAEFIQENTKTDIVDI 104
Cdd:cd04735    66 -EGGFSAD---DDSDipGLRKLAQAIKSKGAKAILQI 98
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 125-234 7.70e-03

monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380621 [Multi-domain]  Cd Length: 278  Bit Score: 37.30  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735078528 125 DPDKIYSIINK--VQSVLDIPLTVKMRTGWSDPSLAVENALAAEAAGVSALAMhgrtreqmyTGHADLETLHKVAQALTK 202
Cdd:cd19966    10 PGDPFWTVVYNgaKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAI---------MGHPGDGAYTPLIEAAKK 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2735078528 203 --IPFI-ANGDIRTVQDAKQRIEEVGADAVMIGRA 234
Cdd:cd19966    81 agIIVTsFNTDLPKLEYGDCGLGYVGADLYAAGYT 115
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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