|
Name |
Accession |
Description |
Interval |
E-value |
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-314 |
1.06e-166 |
|
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: 466.11 E-value: 1.06e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 4 GPYTLDNPLIVAPMAGVTDRPFRTLCKHFGAGHAISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILAEAA 83
Cdd:COG0042 1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 84 RYQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEENILRVAAMAEQAGI 163
Cdd:COG0042 81 RIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDENALEFARIAEDAGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 164 AALAIHGRTREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRHYLQT 243
Cdd:COG0042 161 AALTVHGRTREQRYKGPADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYLAG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2743939927 244 GEtLPPPDVAEIHAVLLQHLDDLYQFYGEYSGCRIARKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVD 314
Cdd:COG0042 241 GE-APPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELLE 310
|
|
| nifR3_yhdG |
TIGR00737 |
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
3-316 |
5.62e-141 |
|
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: 401.36 E-value: 5.62e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 3 IGPYTLDNPLIVAPMAGVTDRPFRTLCKHFGAGHAISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILAEA 82
Cdd:TIGR00737 1 IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLFGSDPDTMAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 83 ARYQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEENILRVAAMAEQAG 162
Cdd:TIGR00737 81 AKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRIGWDDAHINAVEAARIAEDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 163 IAALAIHGRTREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRHYLQ 242
Cdd:TIGR00737 161 AQAVTLHGRTRAQGYSGEANWDIIARVKQAVRIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEQYLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2743939927 243 TGETLPPPDVAEIHAVLLQHLDDLYQFYGEYSGCRIARKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVDAY 316
Cdd:TIGR00737 241 TGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKHIAWYLKGFPGNAALRQTLNHASSFQEVKQLLDDF 314
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
1-320 |
1.48e-139 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 397.80 E-value: 1.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 1 MKIGPYTLDNPLIVAPMAGVTDRPFRTLCKHFGAGHAISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILA 80
Cdd:PRK10415 1 MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 81 EAARYQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEENILRVAAMAEQ 160
Cdd:PRK10415 81 DAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCVEIAQLAED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 161 AGIAALAIHGRTREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRHY 240
Cdd:PRK10415 161 CGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 241 LQTGETLPPPDVAEIHAVLLQHLDDLYQFYGEYSGCRIARKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVDAYLKAL 320
Cdd:PRK10415 241 LDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENF 320
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
13-321 |
1.35e-118 |
|
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: 344.31 E-value: 1.35e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 13 IVAPMAGVTDRPFRTLCKHFGAGH-AISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILAEAARYQVANGA 91
Cdd:pfam01207 1 LLAPMAGVTDLPFRRLVREYGAGDlVYTEMVTAKAQLRPEKVRIRMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 92 QIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEENILRVAAMAEQAGIAALAIHGR 171
Cdd:pfam01207 81 DGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHENAVEIAKIVEDAGAQALTVHGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 172 TREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIrHYLQTGETLPPPD 251
Cdd:pfam01207 161 TRAQNYEGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAEQ-HTVKTGEFGPSPP 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 252 VAEIHAVLLQHLDDLYQFYGEYSGCRIARKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVDAYLKALE 321
Cdd:pfam01207 240 LAEEAEKVLRHLPYLEEFLGEDKGLRHARKHLAWYLKGFPGAAELRRELNDVFDPVEALINLDAALRAAN 309
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
11-241 |
5.84e-110 |
|
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: 319.05 E-value: 5.84e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 11 PLIVAPMAGVTDRPFRTLCKHFGAGHAISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILAEAARYQVANG 90
Cdd:cd02801 1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLAEAAKIVEELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 91 AQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYvNGEENILRVAAMAEQAGIAALAIHG 170
Cdd:cd02801 81 ADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGW-DDEEETLELAKALEDAGASALTVHG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2743939927 171 RTREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRHYL 241
Cdd:cd02801 160 RTREQRYSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELL 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-314 |
1.06e-166 |
|
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: 466.11 E-value: 1.06e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 4 GPYTLDNPLIVAPMAGVTDRPFRTLCKHFGAGHAISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILAEAA 83
Cdd:COG0042 1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 84 RYQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEENILRVAAMAEQAGI 163
Cdd:COG0042 81 RIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDENALEFARIAEDAGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 164 AALAIHGRTREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRHYLQT 243
Cdd:COG0042 161 AALTVHGRTREQRYKGPADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYLAG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2743939927 244 GEtLPPPDVAEIHAVLLQHLDDLYQFYGEYSGCRIARKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVD 314
Cdd:COG0042 241 GE-APPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELLE 310
|
|
| nifR3_yhdG |
TIGR00737 |
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
3-316 |
5.62e-141 |
|
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: 401.36 E-value: 5.62e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 3 IGPYTLDNPLIVAPMAGVTDRPFRTLCKHFGAGHAISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILAEA 82
Cdd:TIGR00737 1 IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLFGSDPDTMAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 83 ARYQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEENILRVAAMAEQAG 162
Cdd:TIGR00737 81 AKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRIGWDDAHINAVEAARIAEDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 163 IAALAIHGRTREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRHYLQ 242
Cdd:TIGR00737 161 AQAVTLHGRTRAQGYSGEANWDIIARVKQAVRIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEQYLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2743939927 243 TGETLPPPDVAEIHAVLLQHLDDLYQFYGEYSGCRIARKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVDAY 316
Cdd:TIGR00737 241 TGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKHIAWYLKGFPGNAALRQTLNHASSFQEVKQLLDDF 314
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
1-320 |
1.48e-139 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 397.80 E-value: 1.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 1 MKIGPYTLDNPLIVAPMAGVTDRPFRTLCKHFGAGHAISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILA 80
Cdd:PRK10415 1 MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 81 EAARYQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEENILRVAAMAEQ 160
Cdd:PRK10415 81 DAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCVEIAQLAED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 161 AGIAALAIHGRTREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRHY 240
Cdd:PRK10415 161 CGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 241 LQTGETLPPPDVAEIHAVLLQHLDDLYQFYGEYSGCRIARKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVDAYLKAL 320
Cdd:PRK10415 241 LDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENF 320
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
13-321 |
1.35e-118 |
|
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: 344.31 E-value: 1.35e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 13 IVAPMAGVTDRPFRTLCKHFGAGH-AISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILAEAARYQVANGA 91
Cdd:pfam01207 1 LLAPMAGVTDLPFRRLVREYGAGDlVYTEMVTAKAQLRPEKVRIRMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 92 QIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEENILRVAAMAEQAGIAALAIHGR 171
Cdd:pfam01207 81 DGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHENAVEIAKIVEDAGAQALTVHGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 172 TREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIrHYLQTGETLPPPD 251
Cdd:pfam01207 161 TRAQNYEGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAEQ-HTVKTGEFGPSPP 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 252 VAEIHAVLLQHLDDLYQFYGEYSGCRIARKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVDAYLKALE 321
Cdd:pfam01207 240 LAEEAEKVLRHLPYLEEFLGEDKGLRHARKHLAWYLKGFPGAAELRRELNDVFDPVEALINLDAALRAAN 309
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
11-241 |
5.84e-110 |
|
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: 319.05 E-value: 5.84e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 11 PLIVAPMAGVTDRPFRTLCKHFGAGHAISEMMTADMTLYAQKKSLYRANFDGELAPVSAQIAGSEPEILAEAARYQVANG 90
Cdd:cd02801 1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLAEAAKIVEELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 91 AQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYvNGEENILRVAAMAEQAGIAALAIHG 170
Cdd:cd02801 81 ADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGW-DDEEETLELAKALEDAGASALTVHG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2743939927 171 RTREQMYTGQARHELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRHYL 241
Cdd:cd02801 160 RTREQRYSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELL 230
|
|
| PRK10550 |
PRK10550 |
tRNA dihydrouridine(16) synthase DusC; |
12-316 |
2.00e-37 |
|
tRNA dihydrouridine(16) synthase DusC;
Pssm-ID: 236713 Cd Length: 312 Bit Score: 135.71 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 12 LIVAPMAGVTDRPFRTLCKHFGA-GHAISEMM-TADMTLYAqkKSLYR-------ANFDGELAPVSAQIAGSEPEILAEA 82
Cdd:PRK10550 3 VLLAPMEGVLDSLVRELLTEVNDyDLCITEFLrVVDQLLPV--KVFHRlcpelhnASRTPSGTLVRIQLLGQYPQWLAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 83 ARYQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAV--DVPVTLKTRLGYVNGEENiLRVAAMAEQ 160
Cdd:PRK10550 81 AARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVTVKVRLGWDSGERK-FEIADAVQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 161 AGIAALAIHGRTREQMYTGQARH-ELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRPWIFREIRH 239
Cdd:PRK10550 160 AGATELVVHGRTKEDGYRAEHINwQAIGEIRQRLTIPVIANGEIWDWQSAQQCMAITGCDAVMIGRGALNIPNLSRVVKY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2743939927 240 ylqTGETLPPPDVAEI--HAVLLQHLDDLyqfyGEYSGCRIaRKHIAWYTNGLHNSNTFRQTMYAQESTAEQARVVDAY 316
Cdd:PRK10550 240 ---NEPRMPWPEVVALlqKYTRLEKQGDT----GLYHVARI-KQWLGYLRKEYDEATELFQEIRALNNSPDIARAIQAI 310
|
|
| PRK11815 |
PRK11815 |
tRNA dihydrouridine(20/20a) synthase DusA; |
1-323 |
3.99e-30 |
|
tRNA dihydrouridine(20/20a) synthase DusA;
Pssm-ID: 236991 [Multi-domain] Cd Length: 333 Bit Score: 116.77 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 1 MKIGPYTLDNPLIVAPMAGVTDRPFRTLCKHFgAGHAI--SEMMTADMTLYAQKKSLYRanFDGELAPVSAQIAGSEPEI 78
Cdd:PRK11815 2 PEKMSKLPSRRFSVAPMMDWTDRHCRYFHRLL-SRHALlyTEMVTTGAIIHGDRERLLA--FDPEEHPVALQLGGSDPAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 79 LAEAARYQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGyVNGEEN--ILR--V 154
Cdd:PRK11815 79 LAEAAKLAEDWGYDEINLNVGCPSDRVQNGRFGACLMAEPELVADCVKAMKDAVSIPVTVKHRIG-IDDQDSyeFLCdfV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 155 AAMAEqAGIAALAIHGRtreqmytgQA----------------RHELIGEVKRSV-HIPIIANGDIDSPQKARQVLDvtG 217
Cdd:PRK11815 158 DTVAE-AGCDTFIVHAR--------KAwlkglspkenreipplDYDRVYRLKRDFpHLTIEINGGIKTLEEAKEHLQ--H 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 218 ADAIMIGRAAQGRPWIFREIRHYLqTGETLPPPDVAEIHAVLLQHLDDlYQFYGEYSGcRIARkHIAWYTNGLHNSNTFR 297
Cdd:PRK11815 227 VDGVMIGRAAYHNPYLLAEVDREL-FGEPAPPLSRSEVLEAMLPYIER-HLAQGGRLN-HITR-HMLGLFQGLPGARAWR 302
|
330 340
....*....|....*....|....*.
gi 2743939927 298 QTMyaqestAEQARVVDAYLKALEAA 323
Cdd:PRK11815 303 RYL------SENAHKPGAGIEVLEEA 322
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
49-243 |
4.19e-14 |
|
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: 71.43 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 49 YAQKKSLYRANFDgelAPVSAQIAGSEPEILAEAARYQVANGAQIVDINMGCPAkkvcRKLAGSALLQDEELVKRILNTV 128
Cdd:cd04740 77 FLEELLPWLREFG---TPVIASIAGSTVEEFVEVAEKLADAGADAIELNISCPN----VKGGGMAFGTDPEAVAEIVKAV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 129 VAAVDVPVTLKtrLG-YVNgeeNILRVAAMAEQAG---------IAALAIHGRTREQM-------YTGQARH----ELIG 187
Cdd:cd04740 150 KKATDVPVIVK--LTpNVT---DIVEIARAAEEAGadgltlintLKGMAIDIETRKPIlgnvtggLSGPAIKpialRMVY 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2743939927 188 EVKRSVHIPIIANGDIDSPQKARQVLdVTGADAIMIGRAAQGRPWIFREIRHYLQT 243
Cdd:cd04740 225 QVYKAVEIPIIGVGGIASGEDALEFL-MAGASAVQVGTANFVDPEAFKEIIEGLEA 279
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
66-237 |
2.66e-13 |
|
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: 69.31 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 66 PVSAQIAGSEPEILAEAARYQVANGAQIVDINMGCPAKKVCRKLagsalLQDEELVKRILNTVVAAVDVPVTLKtrLGYV 145
Cdd:cd02810 100 PLIASVGGSSKEDYVELARKIERAGAKALELNLSCPNVGGGRQL-----GQDPEAVANLLKAVKAAVDIPLLVK--LSPY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 146 NGEENILRVAAMAEQAGIAALA----IHGRTREQMYTGQARHELIGEVK---------RSVH---------IPIIANGDI 203
Cdd:cd02810 173 FDLEDIVELAKAAERAGADGLTaintISGRVVDLKTVGPGPKRGTGGLSgapirplalRWVArlaarlqldIPIIGVGGI 252
|
170 180 190
....*....|....*....|....*....|....*
gi 2743939927 204 DSPQKARQVLDVtGADAIMIGRAAQGR-PWIFREI 237
Cdd:cd02810 253 DSGEDVLEMLMA-GASAVQVATALMWDgPDVIRKI 286
|
|
| arch_FMN |
cd02911 |
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
11-238 |
3.53e-13 |
|
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: 67.74 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 11 PLIVAPMAGVTDRPF-RTLCKHFGA----GHAI-SEMMTA--DMTLYAQKKSLYR---ANFDGELAP-------VSAQIA 72
Cdd:cd02911 1 PVALASMAGITDGDFcRKRADHAGLvflgGYNLdERTIEAarKLVKRGRKEFLPDdplEFIEGEIKAlkdsnvlVGVNVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 73 GSEPEILAEAARyQVANGAQIVDINMGCPAKKVCRKLAGSALLQDEELVKRILnTVVAAVDVPVTLKTRLGYVNGEENIL 152
Cdd:cd02911 81 SSSLEPLLNAAA-LVAKNAAILEINAHCRQPEMVEAGAGEALLKDPERLSEFI-KALKETGVPVSVKIRAGVDVDDEELA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 153 RvaaMAEQAGiaALAIHgrtREQMYTGQ-ARHELIGEVKRSVHipIIANGDIDSPQKARQVLDvTGADAIMIGRAAqgRP 231
Cdd:cd02911 159 R---LIEKAG--ADIIH---VDAMDPGNhADLKKIRDISTELF--IIGNNSVTTIESAKEMFS-YGADMVSVARAS--LP 225
|
....*..
gi 2743939927 232 WIFREIR 238
Cdd:cd02911 226 ENIEWLV 232
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
123-227 |
1.58e-12 |
|
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: 67.21 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 123 RILNTVVAAV------DVPVTLK----TRLGYVNGEENILRVAAMAEQAGIAALAI-------HGRTREQMYTGQARH-E 184
Cdd:cd02803 192 RFLLEIVAAVreavgpDFPVGVRlsadDFVPGGLTLEEAIEIAKALEEAGVDALHVsggsyesPPPIIPPPYVPEGYFlE 271
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2743939927 185 LIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAA 227
Cdd:cd02803 272 LAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRAL 314
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
66-237 |
2.66e-10 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 60.16 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 66 PVSAQIAGSEPEILAEAA-RYQVANGAQIVDINMGCP-AKKvcrklAGSALLQDEELVKRILNTVVAAVDVPVTLKtrLG 143
Cdd:PRK07259 93 PIIANVAGSTEEEYAEVAeKLSKAPNVDAIELNISCPnVKH-----GGMAFGTDPELAYEVVKAVKEVVKVPVIVK--LT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 144 -YVngeENILRVAAMAEQAG---------IAALAIHGRTREQM-------YTGQARH----ELIGEVKRSVHIPIIANGD 202
Cdd:PRK07259 166 pNV---TDIVEIAKAAEEAGadglslintLKGMAIDIKTRKPIlanvtggLSGPAIKpialRMVYQVYQAVDIPIIGMGG 242
|
170 180 190
....*....|....*....|....*....|....*
gi 2743939927 203 IDSPQKARQVLdVTGADAIMIGRAAQGRPWIFREI 237
Cdd:PRK07259 243 ISSAEDAIEFI-MAGASAVQVGTANFYDPYAFPKI 276
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
123-227 |
2.62e-09 |
|
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: 57.87 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 123 RILNTVVAAV------DVPVTLktRL---GYVNG---EENILRVAAMAEQAGIAALAIHGRTRE--QMYTGQARH----E 184
Cdd:COG1902 200 RFLLEVVEAVraavgpDFPVGV--RLsptDFVEGgltLEESVELAKALEEAGVDYLHVSSGGYEpdAMIPTIVPEgyqlP 277
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2743939927 185 LIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAA 227
Cdd:COG1902 278 FAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRPL 320
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
177-226 |
3.70e-06 |
|
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: 47.18 E-value: 3.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2743939927 177 YTGQARH------ELIGEVKRSVHIPIIANGDIDSPQKARQVLDVtGADAIMIGRA 226
Cdd:cd04729 154 YTEETAKtedpdfELLKELRKALGIPVIAEGRINSPEQAAKALEL-GADAVVVGSA 208
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
177-226 |
3.76e-06 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 47.06 E-value: 3.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2743939927 177 YTGQARH------ELIGEVKRSVHIPIIANGDIDSPQKARQVLDVtGADAIMIGRA 226
Cdd:PRK01130 150 YTEETKKpeepdfALLKELLKAVGCPVIAEGRINTPEQAKKALEL-GAHAVVVGGA 204
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
123-235 |
3.62e-05 |
|
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: 44.79 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 123 RILNTVVAAV------DVPVTLktRLG---YVNGEENI---LRVAAMAEQAGIAAL-----AIHGRTREQMYTG-QArhE 184
Cdd:cd02932 205 RFLLEVVDAVravwpeDKPLFV--RISatdWVEGGWDLedsVELAKALKELGVDLIdvssgGNSPAQKIPVGPGyQV--P 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2743939927 185 LIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADAIMIGRAAQGRP-WIFR 235
Cdd:cd02932 281 FAERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVALGRELLRNPyWPLH 332
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
77-136 |
4.05e-05 |
|
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; Methionine synthase I, cobalamin-binding domain is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 441020 [Multi-domain] Cd Length: 1141 Bit Score: 45.33 E-value: 4.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 77 EILAEAaRYQVANGAQIVDINMGCPakkvcrklagsaLLQDEELVKRILNTVVAAVDVPV 136
Cdd:COG1410 359 EALEVA-REQVEAGAQILDVNVDEP------------GRDEVAAMVRFLNLLASEVRVPL 405
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
66-225 |
1.54e-04 |
|
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: 42.19 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 66 PVSAQIAGSEP-EILAEAARYQVANGAQIVDINMGCPAKkvcrklagsallqDEELVKRILNTVVAAVDVPVTLKTRLgy 144
Cdd:cd04722 59 PLGVQLAINDAaAAVDIAAAAARAAGADGVEIHGAVGYL-------------AREDLELIRELREAVPDVKVVVKLSP-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 145 vngeeNILRVAAMAEQAGIAALAIHGRTREQMYTGQAR--HELIGEVKRSVHIPIIANGDIDSPQKARQVLDVtGADAIM 222
Cdd:cd04722 124 -----TGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPiaDLLLILAKRGSKVPVIAGGGINDPEDAAEALAL-GADGVI 197
|
...
gi 2743939927 223 IGR 225
Cdd:cd04722 198 VGS 200
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
184-220 |
5.18e-04 |
|
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: 40.91 E-value: 5.18e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2743939927 184 ELIGEVKRSVHIPIIANGDIDSPQKARQVLDVTGADA 220
Cdd:cd04731 183 ELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADA 219
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
111-226 |
6.03e-04 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (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.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 40.54 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 111 GSALLQDEELVKRILNT-----VVAAVDVpvtlktRLGYV-------NGEENILRVAAMAEQAGIAAL---AIHgrtREQ 175
Cdd:cd04732 102 GTAAVKNPELVKELLKEyggerIVVGLDA------KDGKVatkgwleTSEVSLEELAKRFEELGVKAIiytDIS---RDG 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2743939927 176 MYTGQARhELIGEVKRSVHIPIIANGDIDSPQKARQvLDVTGADAIMIGRA 226
Cdd:cd04732 173 TLSGPNF-ELYKELAAATGIPVIASGGVSSLDDIKA-LKELGVAGVIVGKA 221
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
79-228 |
1.11e-03 |
|
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. 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 the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239244 Cd Length: 299 Bit Score: 40.35 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 79 LAEAAryqvanGAQIVDINMGCPAKKVCRKLaGSALLQDEELVKRILNTVVAAVDVPVTLKTRLGYVNGEEnILRVAAMA 158
Cdd:cd02940 121 LVEEA------GADALELNFSCPHGMPERGM-GAAVGQDPELVEEICRWVREAVKIPVIAKLTPNITDIRE-IARAAKEG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 159 EQAGIAAL------------------AIHGRTREQMYTGQARHEL----IGEVKRSVH--IPIIANGDIDSPQKARQVLd 214
Cdd:cd02940 193 GADGVSAIntvnslmgvdldgtppapGVEGKTTYGGYSGPAVKPIalraVSQIARAPEpgLPISGIGGIESWEDAAEFL- 271
|
170
....*....|....
gi 2743939927 215 VTGADAIMIGRAAQ 228
Cdd:cd02940 272 LLGASVVQVCTAVM 285
|
|
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
81-98 |
3.18e-03 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 39.39 E-value: 3.18e-03
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
163-226 |
3.51e-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: 38.73 E-value: 3.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2743939927 163 IAALAIHGRTREQMYTGQARHELigeVKRSVH--IPIIANGDIDSPQKARQVLDvTGADAIMIGRA 226
Cdd:cd04735 254 ISLWDFDRKSRRGRDDNQTIMEL---VKERIAgrLPLIAVGSINTPDDALEALE-TGADLVAIGRG 315
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
75-195 |
6.07e-03 |
|
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.
Pssm-ID: 238242 [Multi-domain] Cd Length: 258 Bit Score: 37.64 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743939927 75 EPEILAEAARYQVANGAQIVDINM--GCPAKKVCRKlagsallqDEEL--VKRILNTVVAAVDVPVTLKT------RLGY 144
Cdd:cd00423 22 SLDKALEHARRMVEEGADIIDIGGesTRPGAEPVSV--------EEELerVIPVLRALAGEPDVPISVDTfnaevaEAAL 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2743939927 145 ---------VNGEENILRVAAMAEQAGIAALAIH-----GRTREQMYTGQARHELIGEVKRSVHI 195
Cdd:cd00423 94 kagadiindVSGGRGDPEMAPLAAEYGAPVVLMHmdgtpQTMQNNPYYADVVDEVVEFLEERVEA 158
|
|
| PRK04169 |
PRK04169 |
heptaprenylglyceryl phosphate synthase; |
184-224 |
8.32e-03 |
|
heptaprenylglyceryl phosphate synthase;
Pssm-ID: 235237 Cd Length: 232 Bit Score: 37.10 E-value: 8.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2743939927 184 ELIGEVKRSVHI-PIIANGDIDSPQKARQVLDvTGADAIMIG 224
Cdd:PRK04169 173 EMVKAVKKALDItPLIYGGGIRSPEQARELMA-AGADTIVVG 213
|
|
| |
