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Conserved domains on  [gi|1934377680|ref|WP_195579600|]
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nucleoside deaminase [Alistipes shahii]

Protein Classification

nucleoside deaminase( domain architecture ID 10001752)

nucleoside deaminase such as adenosine, guanine, or cytosine deaminase is a Zn-dependent enzyme which catalyzes 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

EC:  3.5.4.-
Gene Ontology:  GO:0008270|GO:0019239|GO:0009116
PubMed:  38524700
SCOP:  3001838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 5-144 7.84e-46

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: 146.03  E-value: 7.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680   5 ETDEKFMRLALNEAQKALKQQEVPigavvvaggavigRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVE 84
Cdd:COG0590     2 EDDEEFMRRALELARKAVAEGEVPvgavlvkdgeiiaRGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934377680  85 PCIMCAGAIGWAQVSRVVWGADDPKKG-----FRRYSEAVFHPRTTVARGVLREECEELMSGFFA 144
Cdd:COG0590    82 PCPMCAGAIVWARIGRVVYGASDPKAGaagsiYDLLADPRLNHRVEVVGGVLAEECAALLRDFFA 146
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 5-144 7.84e-46

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: 146.03  E-value: 7.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680   5 ETDEKFMRLALNEAQKALKQQEVPigavvvaggavigRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVE 84
Cdd:COG0590     2 EDDEEFMRRALELARKAVAEGEVPvgavlvkdgeiiaRGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934377680  85 PCIMCAGAIGWAQVSRVVWGADDPKKG-----FRRYSEAVFHPRTTVARGVLREECEELMSGFFA 144
Cdd:COG0590    82 PCPMCAGAIVWARIGRVVYGASDPKAGaagsiYDLLADPRLNHRVEVVGGVLAEECAALLRDFFA 146
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 11-111 2.68e-28

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: 100.38  E-value: 2.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680  11 MRLALNEAQKALKQQEVPIGAV-VVAGGAVIGRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVEPCIMC 89
Cdd:cd01285     1 MRLAIELARKALAEGEVPFGAViVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                          90       100
                  ....*....|....*....|..
gi 1934377680  90 AGAIGWAQVSRVVWGADDPKKG 111
Cdd:cd01285    81 AGALLWARIKRVVYGASDPKLG 102
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 5-147 2.10e-26

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: 96.82  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680   5 ETDEKFMRLALNEAQKALKQQEVPIGAVVVAGGAVIGRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVE 84
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934377680  85 PCIMCAGAIGWAQVSRVVWGADDPKKGFRRY--SEAVFHpRTTVARGVLREECEELMSGFFAGLR 147
Cdd:pfam14437  81 PCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSvlNKLVIV-LWNHRVELVEEDCSEILKGFFKKLR 144
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 7-143 1.15e-23

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 90.64  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680   7 DEKFMRLALNEAQKALKQQEVPIGAVVVAGGAVIGRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVEPC 86
Cdd:PRK10860   13 HEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPC 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934377680  87 IMCAGAIGWAQVSRVVWGADDPKKGFR-RYSEAVFHP----RTTVARGVLREECEELMSGFF 143
Cdd:PRK10860   93 VMCAGAMVHSRIGRLVFGARDAKTGAAgSLMDVLHHPgmnhRVEITEGVLADECAALLSDFF 154
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 78-148 2.73e-05

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: 42.51  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680  78 TLYVTVEPCIM------CAGAIGWAQVSRVVWGADDPK-----KGFRRYSEAVFHprttVARGVLREECEELMSGFFAGL 146
Cdd:TIGR00326  61 TAYVTLEPCSHqgrtppCAEAIIEAGIKKVVVSMQDPNplvagRGAERLKQAGIE----VTFGILKEEAERLNKGFLKRM 136


                  ..
gi 1934377680 147 RG 148
Cdd:TIGR00326 137 RT 138
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 5-144 7.84e-46

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: 146.03  E-value: 7.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680   5 ETDEKFMRLALNEAQKALKQQEVPigavvvaggavigRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVE 84
Cdd:COG0590     2 EDDEEFMRRALELARKAVAEGEVPvgavlvkdgeiiaRGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934377680  85 PCIMCAGAIGWAQVSRVVWGADDPKKG-----FRRYSEAVFHPRTTVARGVLREECEELMSGFFA 144
Cdd:COG0590    82 PCPMCAGAIVWARIGRVVYGASDPKAGaagsiYDLLADPRLNHRVEVVGGVLAEECAALLRDFFA 146
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 11-111 2.68e-28

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: 100.38  E-value: 2.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680  11 MRLALNEAQKALKQQEVPIGAV-VVAGGAVIGRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVEPCIMC 89
Cdd:cd01285     1 MRLAIELARKALAEGEVPFGAViVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                          90       100
                  ....*....|....*....|..
gi 1934377680  90 AGAIGWAQVSRVVWGADDPKKG 111
Cdd:cd01285    81 AGALLWARIKRVVYGASDPKLG 102
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 5-147 2.10e-26

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: 96.82  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680   5 ETDEKFMRLALNEAQKALKQQEVPIGAVVVAGGAVIGRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVE 84
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934377680  85 PCIMCAGAIGWAQVSRVVWGADDPKKGFRRY--SEAVFHpRTTVARGVLREECEELMSGFFAGLR 147
Cdd:pfam14437  81 PCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSvlNKLVIV-LWNHRVELVEEDCSEILKGFFKKLR 144
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 7-143 1.15e-23

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 90.64  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680   7 DEKFMRLALNEAQKALKQQEVPIGAVVVAGGAVIGRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVEPC 86
Cdd:PRK10860   13 HEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPC 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934377680  87 IMCAGAIGWAQVSRVVWGADDPKKGFR-RYSEAVFHP----RTTVARGVLREECEELMSGFF 143
Cdd:PRK10860   93 VMCAGAMVHSRIGRLVFGARDAKTGAAgSLMDVLHHPgmnhRVEITEGVLADECAALLSDFF 154
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
6-104 3.43e-20

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 79.27  E-value: 3.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680   6 TDEKFMRLALNEAQKALKQQEVPI-GAVVVAGGAVIGRGHNLVETLADPTAHAEMQALTAAAATLGGKYLQECTLYVTVE 84
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSNFPVgAVIVKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLE 80

                          90       100
                  ....*....|....*....|
gi 1934377680  85 PCIMCAGAIGWAQVSRVVWG 104
Cdd:pfam00383  81 PCGMCAQAIIESGIKRVVFG 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 74-143 1.20e-10

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: 57.76  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680  74 LQECTLYVTVEPCIM------CAGAIGWAQVSRVVWGADDP-----KKGFRRYSEAvfhpRTTVARGVLREECEELMSGF 142
Cdd:COG0117    60 ARGATLYVTLEPCSHhgrtppCADALIEAGIKRVVIAMLDPnplvaGKGIARLRAA----GIEVEVGVLEEEARALNRGF 135


                  .
gi 1934377680 143 F 143
Cdd:COG0117   136 L 136
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 78-148 2.73e-05

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: 42.51  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680  78 TLYVTVEPCIM------CAGAIGWAQVSRVVWGADDPK-----KGFRRYSEAVFHprttVARGVLREECEELMSGFFAGL 146
Cdd:TIGR00326  61 TAYVTLEPCSHqgrtppCAEAIIEAGIKKVVVSMQDPNplvagRGAERLKQAGIE----VTFGILKEEAERLNKGFLKRM 136


                  ..
gi 1934377680 147 RG 148
Cdd:TIGR00326 137 RT 138
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 77-120 3.41e-05

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: 41.11  E-value: 3.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1934377680  77 CTLYVTVEPCIMCAGAIGWAQVSRVVwgADDPKKGFRRYSEAVF 120
Cdd:cd01286    89 ATLYVTLFPCIECAKLIIQAGIKKVV--YAEPYDDDDPAAAELL 130
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 42-102 6.82e-05

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: 39.46  E-value: 6.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934377680  42 RGHNLVETLADPTAHAEMQALTAAAATLGGKYlqeCTLYVTVEPCIMCAGAIGWAQVSRVV 102
Cdd:cd00786    35 RGCNIENAAYSMCNHAERTALFNAGSEGDTKG---QMLYVALSPCGACAQLIIELGIKDVI 92
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
77-102 7.15e-05

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 40.59  E-value: 7.15e-05
                          10        20
                  ....*....|....*....|....*.
gi 1934377680  77 CTLYVTVEPCIMCAGAIGWAQVSRVV 102
Cdd:COG2131    99 ATLYVTHFPCLECAKMIIQAGIKRVV 124
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 78-147 3.24e-04

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 39.36  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680  78 TLYVTVEPCIM------CAGAIGWAQVSRVVWGADDPK-----KGFRRYSEAvfhpRTTVARGVLREECEELMSGFFAGL 146
Cdd:PRK10786   67 TAYVTLEPCSHhgrtppCCDALIAAGVARVVAAMQDPNpqvagRGLYRLQQA----GIDVSHGLMMSEAEALNKGFLKRM 142


                  .
gi 1934377680 147 R 147
Cdd:PRK10786  143 R 143
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 49-118 1.09e-03

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: 36.44  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934377680  49 TLADPTAHAEMQALTAAAAtlggKYLQECTLYVTVEPCIM------CAGAIGWAQVSRVVWGADDP-----KKGFRRYSE 117
Cdd:cd01284    38 HRKAGGPHAEVNALASAGE----KLARGATLYVTLEPCSHhgktppCVDAIIEAGIKRVVVGVRDPnplvaGKGAERLRA 113


                  .
gi 1934377680 118 A 118
Cdd:cd01284   114 A 114
 
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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