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Conserved domains on  [gi|613027546|gb|EZW37189|]
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riboflavin biosynthesis protein RibD [Staphylococcus aureus 43P3]

Protein Classification

dihydrofolate reductase family protein( domain architecture ID 106942)

dihydrofolate reductase family protein; similar to Lacticaseibacillus rhamnosus dihydrofolate reductase which reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHFR super family cl17279
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
 5-343 3.86e-94

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


The actual alignment was detected with superfamily member TIGR00326:

Pssm-ID: 473077 [Multi-domain]  Cd Length: 344  Bit Score: 284.03  E-value: 3.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546    5 MDYAIQLANMVQGQTGVNPPVGAVVVKEGRIVGIGAHLRKGDKHAEVQALDMAQQNAEGATIYITLEPCSHFGSTPPCVN 84
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   85 KIIDCKIAKVVYATKD-NSLDT-HGDETLRDHGIEVEC-VDDERASQLYQDFFKAKAKQLPQITVKVSASLDGKQANDNG 161
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDpNPLVAgRGAERLKQAGIEVTFgILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  162 QSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQDGKN-PIKVILSKSGNIHFNQQIYQDEStPIWIYTEN 240
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATEqPLRVVLDTQLRIPEFAKLIPQIA-PTWIFTTA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  241 PNLTT--NQTHIEIIYLKSCDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQSNYIDEFILYYAPKLIGGSGNYQFYQTND 318
Cdd:TIGR00326 240 RDKKKrlEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLLGGTHAPGLCSEPG 319

                         330       340
                  ....*....|....*....|....*
gi 613027546  319 VIEIPDANQFEIVHSELLNQNVKLT 343
Cdd:TIGR00326 320 FQKMADALNFKFLEINQIGPDILLT 344
 
Name Accession Description Interval E-value
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 5-343 3.86e-94

riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273015 [Multi-domain]  Cd Length: 344  Bit Score: 284.03  E-value: 3.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546    5 MDYAIQLANMVQGQTGVNPPVGAVVVKEGRIVGIGAHLRKGDKHAEVQALDMAQQNAEGATIYITLEPCSHFGSTPPCVN 84
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   85 KIIDCKIAKVVYATKD-NSLDT-HGDETLRDHGIEVEC-VDDERASQLYQDFFKAKAKQLPQITVKVSASLDGKQANDNG 161
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDpNPLVAgRGAERLKQAGIEVTFgILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  162 QSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQDGKN-PIKVILSKSGNIHFNQQIYQDEStPIWIYTEN 240
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATEqPLRVVLDTQLRIPEFAKLIPQIA-PTWIFTTA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  241 PNLTT--NQTHIEIIYLKSCDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQSNYIDEFILYYAPKLIGGSGNYQFYQTND 318
Cdd:TIGR00326 240 RDKKKrlEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLLGGTHAPGLCSEPG 319

                         330       340
                  ....*....|....*....|....*
gi 613027546  319 VIEIPDANQFEIVHSELLNQNVKLT 343
Cdd:TIGR00326 320 FQKMADALNFKFLEINQIGPDILLT 344
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 3-238 2.31e-93

Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439887 [Multi-domain]  Cd Length: 311  Bit Score: 280.79  E-value: 2.31e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   3 QFMDYAIQLANMVQGQTGVNPPVGAVVVKEGRIVGIGAHLRKGDKHAEVQALDMAQQNAEGATIYITLEPCSHFGSTPPC 82
Cdd:COG0117    2 RYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPPC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  83 VNKIIDCKIAKVVYATKD-NSL-DTHGDETLRDHGIEVEC-VDDERASQLYQDFFKAKAKQLPQITVKVSASLDGKQAND 159
Cdd:COG0117   82 ADALIEAGIKRVVIAMLDpNPLvAGKGIARLRAAGIEVEVgVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613027546 160 NGQSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQDGKNPIKVILSKSGNIHFNQQIYQDESTPIWIYT 238
Cdd:COG0117  162 NGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALIIV 240
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 4-347 6.53e-71

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 225.03  E-value: 6.53e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   4 FMDYAIQLANMVQGQTGVNPPVGAVVVKEGRIVGIGAHLRKGDKHAEVQALDMAQQNAEGATIYITLEPCSHFGSTPPCV 83
Cdd:PRK10786   6 YMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTPPCC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  84 NKIIDCKIAKVVYATKDNSLDTHGD--ETLRDHGIEVE-CVDDERASQLYQDFFKAKAKQLPQITVKVSASLDGKQANDN 160
Cdd:PRK10786  86 DALIAAGVARVVAAMQDPNPQVAGRglYRLQQAGIDVShGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTAMAS 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 161 GQSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQD-------------GKNPIKVILSKSGNIHFNQQIY 227
Cdd:PRK10786 166 GESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSEldaqtqalypqenLRQPVRIVIDSQNRVTPEHRIV 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 228 QdESTPIWIYTENPNLTTNQTHIEIIYLKS----CDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQSNYIDEFILYYAPK 303
Cdd:PRK10786 246 Q-QPGETWLARTQEDSREWPETVRTLLLPEhnghLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVYIAPK 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 613027546 304 LIGGSGNYQFyQTNDVIEIPDANQFEIVHSELLNQNVKLTLRKK 347
Cdd:PRK10786 325 LLGSDARGLC-TLPGLEKLADAPQFKFSEIRHVGPDVCLHLVPA 367
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 5-115 8.25e-46

Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain.


Pssm-ID: 238611 [Multi-domain]  Cd Length: 115  Bit Score: 152.00  E-value: 8.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   5 MDYAIQLANMVQGQTGVNPPVGAVVVK-EGRIVGIGAHLRKGDKHAEVQALDMAQQN-AEGATIYITLEPCSHFGSTPPC 82
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 613027546  83 VNKIIDCKIAKVVYATKDNslDTH----GDETLRDHG 115
Cdd:cd01284   81 VDAIIEAGIKRVVVGVRDP--NPLvagkGAERLRAAG 115
RibD_C pfam01872
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ...
 142-309 1.54e-40

RibD C-terminal domain; The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG, in combination with pfam00383, as well as in isolation in some archaebacterial proteins. This family appears to be related to pfam00186.


Pssm-ID: 396444  Cd Length: 196  Bit Score: 140.98  E-value: 1.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  142 PQITVKVSASLDGKQANDNGQSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQDG----KNPIKVILSKS 217
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGraaeRQPPRVVVDST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  218 GNIHFNQQIYQDESTPIWIYTENPNLTTNQtHIEIIYLkscDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQSNYIDEFI 297
Cdd:pfam01872  81 LRVPLDARVLNDDAPTLVATTEPADKEKVE-KLKVLRV---DLKELLRELKERGIRSLLVEGGATLAGSLLRAGLVDELR 156

                         170
                  ....*....|..
gi 613027546  298 LYYAPKLIGGSG 309
Cdd:pfam01872 157 LYIAPKLLGGGG 168
 
Name Accession Description Interval E-value
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 5-343 3.86e-94

riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273015 [Multi-domain]  Cd Length: 344  Bit Score: 284.03  E-value: 3.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546    5 MDYAIQLANMVQGQTGVNPPVGAVVVKEGRIVGIGAHLRKGDKHAEVQALDMAQQNAEGATIYITLEPCSHFGSTPPCVN 84
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   85 KIIDCKIAKVVYATKD-NSLDT-HGDETLRDHGIEVEC-VDDERASQLYQDFFKAKAKQLPQITVKVSASLDGKQANDNG 161
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDpNPLVAgRGAERLKQAGIEVTFgILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  162 QSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQDGKN-PIKVILSKSGNIHFNQQIYQDEStPIWIYTEN 240
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATEqPLRVVLDTQLRIPEFAKLIPQIA-PTWIFTTA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  241 PNLTT--NQTHIEIIYLKSCDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQSNYIDEFILYYAPKLIGGSGNYQFYQTND 318
Cdd:TIGR00326 240 RDKKKrlEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLLGGTHAPGLCSEPG 319

                         330       340
                  ....*....|....*....|....*
gi 613027546  319 VIEIPDANQFEIVHSELLNQNVKLT 343
Cdd:TIGR00326 320 FQKMADALNFKFLEINQIGPDILLT 344
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 3-238 2.31e-93

Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439887 [Multi-domain]  Cd Length: 311  Bit Score: 280.79  E-value: 2.31e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   3 QFMDYAIQLANMVQGQTGVNPPVGAVVVKEGRIVGIGAHLRKGDKHAEVQALDMAQQNAEGATIYITLEPCSHFGSTPPC 82
Cdd:COG0117    2 RYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPPC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  83 VNKIIDCKIAKVVYATKD-NSL-DTHGDETLRDHGIEVEC-VDDERASQLYQDFFKAKAKQLPQITVKVSASLDGKQAND 159
Cdd:COG0117   82 ADALIEAGIKRVVIAMLDpNPLvAGKGIARLRAAGIEVEVgVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613027546 160 NGQSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQDGKNPIKVILSKSGNIHFNQQIYQDESTPIWIYT 238
Cdd:COG0117  162 NGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALIIV 240
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 4-347 6.53e-71

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 225.03  E-value: 6.53e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   4 FMDYAIQLANMVQGQTGVNPPVGAVVVKEGRIVGIGAHLRKGDKHAEVQALDMAQQNAEGATIYITLEPCSHFGSTPPCV 83
Cdd:PRK10786   6 YMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTPPCC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  84 NKIIDCKIAKVVYATKDNSLDTHGD--ETLRDHGIEVE-CVDDERASQLYQDFFKAKAKQLPQITVKVSASLDGKQANDN 160
Cdd:PRK10786  86 DALIAAGVARVVAAMQDPNPQVAGRglYRLQQAGIDVShGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTAMAS 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 161 GQSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQD-------------GKNPIKVILSKSGNIHFNQQIY 227
Cdd:PRK10786 166 GESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSEldaqtqalypqenLRQPVRIVIDSQNRVTPEHRIV 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 228 QdESTPIWIYTENPNLTTNQTHIEIIYLKS----CDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQSNYIDEFILYYAPK 303
Cdd:PRK10786 246 Q-QPGETWLARTQEDSREWPETVRTLLLPEhnghLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVYIAPK 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 613027546 304 LIGGSGNYQFyQTNDVIEIPDANQFEIVHSELLNQNVKLTLRKK 347
Cdd:PRK10786 325 LLGSDARGLC-TLPGLEKLADAPQFKFSEIRHVGPDVCLHLVPA 367
RibD COG1985
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ...
 139-347 1.93e-59

Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine reductase, riboflavin biosynthesis is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 441588  Cd Length: 217  Bit Score: 190.76  E-value: 1.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 139 KQLPQITVKVSASLDGKQANDNGQSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQD-GKNPIKVILSKS 217
Cdd:COG1985    1 TGRPYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPGlGRQPLRVVVDSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 218 GNIHFNQQIYQDeSTPIWIYTENPNLTTN-----QTHIEIIYLKS---CDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQ 289
Cdd:COG1985   81 LRLPPDARLFDD-AAPTLVLTTEAADAERraaleAAGAEVIVLPGdgrVDLAALLAALAERGIRSVLVEGGPTLAGSFLA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 613027546 290 SNYIDEFILYYAPKLIGGSGnYQFYQTNDVIEIPDANQFEIVHSELLNQNVKLTLRKK 347
Cdd:COG1985  160 AGLVDELILYIAPKLLGGDG-PTLVGGPGLETLADAPRLRLVSVRRLGDDLLLRYRPR 216
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 5-115 8.25e-46

Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain.


Pssm-ID: 238611 [Multi-domain]  Cd Length: 115  Bit Score: 152.00  E-value: 8.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   5 MDYAIQLANMVQGQTGVNPPVGAVVVK-EGRIVGIGAHLRKGDKHAEVQALDMAQQN-AEGATIYITLEPCSHFGSTPPC 82
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 613027546  83 VNKIIDCKIAKVVYATKDNslDTH----GDETLRDHG 115
Cdd:cd01284   81 VDAIIEAGIKRVVVGVRDP--NPLvagkGAERLRAAG 115
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 2-295 1.62e-44

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 156.86  E-value: 1.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   2 SQFMDYAIQLANMVQGQTGVNPPVGAVVVKEGRIVGIGAHLRKGDKHAEVQALDMAQQNAEGATIYITLEPCSHFGSTPP 81
Cdd:PLN02807  33 SFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLAENATAYVSLEPCNHYGRTPP 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  82 CVNKIIDCKIAKVVYATKD-NSL-DTHGDETLRDHGIEVE-CVDDERASQLYQDFFKAKAKQLPQITVKVSASLDGKQAN 158
Cdd:PLN02807 113 CTEALIKAKVKRVVVGMVDpNPIvASKGIERLRDAGIEVTvGVEEELCRKLNEAFIHRMLTGKPFVTLRYSMSMNGCLLN 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 159 DNGQSqwitnKEVKQDVY-KLRHRHDAVLTGrRTVELDDPQYTTRIQDGKNPIKVILSKSGNIHFNQQIYQDESTP-IWI 236
Cdd:PLN02807 193 QIGEG-----ADDAGGYYsQLLQEYDAVILS-SALADADPLPLSQEAGAKQPLRIIIARSESSPLQIPSLREESAAkVLV 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613027546 237 YTENPNL---TTNQTHIEIIYLKSCDLTTILHNLYKRGVGTLLVEA-GPTTTSEFLQSNYIDE 295
Cdd:PLN02807 267 LADKESSaepVLRRKGVEVVVLNQINLDSILDLCYQRGLCSVLLDLrGNVGGLESLLKDALED 329
ribD_Cterm TIGR00227
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ...
 140-345 9.25e-44

riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases have a zinc-binding domain recognized by the dCMP_cyt_deam model toward the N-terminus and this domain toward the C-terminus. Yeast HTP reductase, a riboflavin-biosynthetic enzyme, and several archaeal proteins believed related to riboflavin biosynthesis consist only of this domain and lack the dCMP_cyt_deam domain.


Pssm-ID: 129330 [Multi-domain]  Cd Length: 216  Bit Score: 150.23  E-value: 9.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  140 QLPQITVKVSASLDGKQANDNGQSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTR---IQDGKNPIKVILSK 216
Cdd:TIGR00227   1 GRPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRwveLDELRNPVRVVLDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  217 SGNIHFNQQIYQDEStPIWIYTENP-NLTTNQTH----IEIIYL--KSCDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQ 289
Cdd:TIGR00227  81 RLRVPPTARLLNDDA-PTWVATSEPaDEEKVKELedfgVEVLVLetKRVDLKKLMEILYEEGIRSVMVEGGGTLNGSLLK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 613027546  290 SNYIDEFILYYAPKLIGGSGNYQFYQTNDVIEIPDANQFEIVHSELLNQNVKLTLR 345
Cdd:TIGR00227 160 EGLVDELIVYIAPKLLGGRDAPTLVDGEGFQKMADAPNLELKEIYQIGEDIVLTAK 215
RibD_C pfam01872
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ...
 142-309 1.54e-40

RibD C-terminal domain; The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG, in combination with pfam00383, as well as in isolation in some archaebacterial proteins. This family appears to be related to pfam00186.


Pssm-ID: 396444  Cd Length: 196  Bit Score: 140.98  E-value: 1.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  142 PQITVKVSASLDGKQANDNGQSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYTTRIQDG----KNPIKVILSKS 217
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGraaeRQPPRVVVDST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  218 GNIHFNQQIYQDESTPIWIYTENPNLTTNQtHIEIIYLkscDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQSNYIDEFI 297
Cdd:pfam01872  81 LRVPLDARVLNDDAPTLVATTEPADKEKVE-KLKVLRV---DLKELLRELKERGIRSLLVEGGATLAGSLLRAGLVDELR 156

                         170
                  ....*....|..
gi 613027546  298 LYYAPKLIGGSG 309
Cdd:pfam01872 157 LYIAPKLLGGGG 168
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-137 5.64e-26

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 100.96  E-value: 5.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   1 MSQFMDYAIQLA--NMVQGqtGVnpPVGAVVVKEGRIVGIGAHLRKGDK----HAEVQALDMAQQNA-----EGATIYIT 69
Cdd:COG0590    4 DEEFMRRALELArkAVAEG--EV--PVGAVLVKDGEIIARGHNRVETLNdptaHAEILAIRAAARKLgnwrlSGCTLYVT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613027546  70 LEPCshfgstPPCVNKIIDCKIAKVVYATKDN------SLDTHGDETLRDHGIEVE-CVDDERASQLYQDFFKAK 137
Cdd:COG0590   80 LEPC------PMCAGAIVWARIGRVVYGASDPkagaagSIYDLLADPRLNHRVEVVgGVLAEECAALLRDFFAAR 148
PRK05625 PRK05625
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
 142-347 1.13e-23

5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated


Pssm-ID: 180169  Cd Length: 217  Bit Score: 96.85  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 142 PQITVKVSASLDGKQANDNGqSQWITNKEVKQDVYKLRHRHDAVLTGRRTVELDDPQYT-TRIQDGK--NPIKVILSKSG 218
Cdd:PRK05625   3 PYVIVNAAMSADGKLATKTR-YSRISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTvHRYAAGKpeNPIRVVVDSSA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 219 NIHFNQQIYQDESTPIwIYTENPNLTTNQT-----HIEIIY--LKSCDLTTILHNLYKRGVGTLLVEAGPTTTSEFLQSN 291
Cdd:PRK05625  82 RTPPDARILDGPAKTI-VAVSEAAPSEKVEelekkGAEVIVagGERVDLPDLLEDLYERGIKRLMVEGGGTLIWSMFKEG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 613027546 292 YIDEFILYYAPKLIGGSGNYQFYQTNDVIEIPDANQFEIVHSELLNQNVKLTLRKK 347
Cdd:PRK05625 161 LVDEVRVTVGPKIIGGKDAPTLADGEGFIEEEDPLKLELAKVCRCDEGVVLTYKVK 216
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
2-97 3.73e-17

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 75.80  E-value: 3.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546    2 SQFMDYAIQLANMvqGQTGVNPPVGAVVVKE-GRIVGIGAH--LRKGDK--HAEVQALDMA-----QQNAEGATIYITLE 71
Cdd:pfam00383   3 EYFMRLALKAAKR--AYPYSNFPVGAVIVKKdGEIIATGYNgeNAGYDPtiHAERNAIRQAgkrgeGVRLEGATLYVTLE 80

                          90       100
                  ....*....|....*....|....*.
gi 613027546   72 PCSHfgstppCVNKIIDCKIAKVVYA 97
Cdd:pfam00383  81 PCGM------CAQAIIESGIKRVVFG 100
PRK14719 PRK14719
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
 141-345 5.32e-15

bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional


Pssm-ID: 237801 [Multi-domain]  Cd Length: 360  Bit Score: 74.97  E-value: 5.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 141 LPQITVKVSASLDGKQANDNGQSQWITNKEVKQdVYKLRHRHDAVLTGRRTVELDDPQYTTRIQDG---KNPIKVILSKS 217
Cdd:PRK14719 139 LPYVISNVGMTLDGKLATIENDSRISGENDLKR-VHEIRKDVDAIMVGIGTVLKDDPRLTVHKINAspkDNPLRIVVDSN 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 218 GNIHFNQQIYQDESTPIwIYTENPNLTTNQTHIE------IIYL----KSCDLTTILHNLYKRGVGTLLVEAGPTTTSEF 287
Cdd:PRK14719 218 LKIPLNARVLNKDAKTV-IATTTPISDEKEEKIRklkemgITVLqagvQKVDLRKIMNEIYKMGINKILLEGGGTLNWGM 296

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 613027546 288 LQSNYIDEFILYYAPKLIGGSGNYQFYQTNDVIEIPDANQFEIVHSELLNQNVKLTLR 345
Cdd:PRK14719 297 FKENLINEVRVYIAPKVFGGANSPTYVDGEGFKNVEECTKLELKNYYPLDDGIVLEYR 354
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
6-124 1.64e-14

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 70.25  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   6 DYAIQLANMVQGQ-TGVNPPVGAVVVKEGRIVGIG--------------AHLRKGDK-------------HAEVQALDMA 57
Cdd:COG2131   10 EYFMEIAKLVALRsTCLRRQVGAVIVKDKRILATGyngapsglphcdevGCLREKLGipsgergeccrtvHAEQNAILQA 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  58 QQN---AEGATIYITLEPCSHfgstppCVNKIIDCKIAKVVYATKDNslDTHGDETLRDHGIEVECVDDE 124
Cdd:COG2131   90 ARHgvsTEGATLYVTHFPCLE------CAKMIIQAGIKRVVYLEDYP--DELAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 25-98 1.93e-12

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 63.45  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  25 VGAVVVKEGRIVGIG--------------AHLRKGDK-----------HAEVQALDMAQQN---AEGATIYITLEPCSHf 76
Cdd:cd01286   22 VGAVIVKDKRIISTGyngspsglphcaevGCERDDLPsgedqkccrtvHAEQNAILQAARHgvsLEGATLYVTLFPCIE- 100

                         90       100
                 ....*....|....*....|..
gi 613027546  77 gstppCVNKIIDCKIAKVVYAT 98
Cdd:cd01286  101 -----CAKLIIQAGIKKVVYAE 117
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 5-97 3.48e-12

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 61.80  E-value: 3.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   5 MDYAIQLANMVQgQTGVNPPVGAVVV--KEGRIVGIGAHLR----KGDKHAEVQALDMAQQNA--EGATIYITLEPCSHf 76
Cdd:cd00786    1 MTEALKAADLGY-AKESNFQVGACLVnkKDGGKVGRGCNIEnaaySMCNHAERTALFNAGSEGdtKGQMLYVALSPCGA- 78

                         90       100
                 ....*....|....*....|.
gi 613027546  77 gstppCVNKIIDCKIAKVVYA 97
Cdd:cd00786   79 -----CAQLIIELGIKDVIVV 94
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 24-136 4.60e-12

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 62.93  E-value: 4.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   24 PVGAVVVKEGRIVGIGAHLRKGDK----HAEVQALDMAQQ-----NAEGATIYITLEPCshfgstPPCVNKIIDCKIAKV 94
Cdd:pfam14437  24 PIGAVIVKDGKVIARGYNRKELNAdttaHAEILAIQQAAKklgswRLDDATLYVTLEPC------PMCAGAIVQAGLKSL 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 613027546   95 VYATKDNSLDTHGDE----TLRDHGIEVECVDDErASQLYQDFFKA 136
Cdd:pfam14437  98 VYGAGNPKGGAVGSVlnklVIVLWNHRVELVEED-CSEILKGFFKK 142
cd PHA02588
deoxycytidylate deaminase; Provisional
 2-130 8.72e-12

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 62.85  E-value: 8.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   2 SQFMDYAIQLAnmvQGQTGVNPPVGAVVVKEGRIVGIGA------------HLRKGDK---------------------- 47
Cdd:PHA02588   4 STYLQIAYLVS---QESKCVSWKVGAVIEKNGRIISTGYngtpaggvnccdHANEQGWlddegklkkehrpehsawsskn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546  48 --HAEVQALDMAQQNA---EGATIYITLEPCshfgstPPCVNKIIDCKIAKVVYATKDNSLDTHGDETLRDHGIEVECVD 122
Cdd:PHA02588  81 eiHAELNAILFAARNGisiEGATMYVTASPC------PDCAKAIAQSGIKKLVYCEKYDRNGPGWDDILRKSGIEVIQIP 154


                 ....*...
gi 613027546 123 DERASQLY 130
Cdd:PHA02588 155 KEELNKLN 162
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 4-140 2.14e-11

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 61.75  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   4 FMDYAIQLANMVQGQTGVnpPVGAVVVKEGRIVG------IGAHlrKGDKHAEVQAL---DMAQQNAE--GATIYITLEP 72
Cdd:PRK10860  16 WMRHALTLAKRAWDEREV--PVGAVLVHNNRVIGegwnrpIGRH--DPTAHAEIMALrqgGLVLQNYRllDATLYVTLEP 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613027546  73 CSHfgstppCVNKIIDCKIAKVVYATKDNSLDTHGD--ETLR----DHGIEV-ECVDDERASQLYQDFFKAKAKQ 140
Cdd:PRK10860  92 CVM------CAGAMVHSRIGRLVFGARDAKTGAAGSlmDVLHhpgmNHRVEItEGVLADECAALLSDFFRMRRQE 160
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 5-101 4.29e-11

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 59.17  E-value: 4.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546   5 MDYAIQLANMVQGQTGVnpPVGAVVV-KEGRIVGIGAHLRKGDK----HAEVQALDMAQQN-----AEGATIYITLEPCs 74
Cdd:cd01285    1 MRLAIELARKALAEGEV--PFGAVIVdDDGKVIARGHNRVEQDGdptaHAEIVAIRNAARRlgsylLSGCTLYTTLEPC- 77

                         90       100
                 ....*....|....*....|....*..
gi 613027546  75 hfgstPPCVNKIIDCKIAKVVYATKDN 101
Cdd:cd01285   78 -----PMCAGALLWARIKRVVYGASDP 99
PRK14059 PRK14059
pyrimidine reductase family protein;
150-307 1.32e-03

pyrimidine reductase family protein;


Pssm-ID: 184482  Cd Length: 251  Bit Score: 39.95  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 150 ASLDGKqANDNGQSQWITNkEVKQDVY-KLRHRHDAVLTGRRTV--------ELDDPQYTTRIQDGKNPIKVI--LSKSG 218
Cdd:PRK14059  39 TSLDGA-ATVDGRSGGLGG-PADRRVFgLLRALADVVVVGAGTVraenyggvRLSAAARQQRQARGQAEVPPIavVSRSG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613027546 219 NIHFNQQIYQD-ESTPIWIYTENPNLTTNQTHIEIIYLKSC--------DLTTILHNLYKRGVGTLLVEAGPTTTSEFLQ 289
Cdd:PRK14059 117 DLDPDSRLFTEtEVPPLVLTCAAAAADRRRRLAGLAEVADVvvagpdtvDLAAAVAALAARGLRRILCEGGPTLLGQLLA 196

                        170
                 ....*....|....*...
gi 613027546 290 SNYIDEFILYYAPKLIGG 307
Cdd:PRK14059 197 ADLVDELCLTIAPVLAGG 214
 
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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