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Conserved domains on  [gi|492422344|ref|WP_005839017|]
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MULTISPECIES: 6-carboxytetrahydropterin synthase QueD [Bacteroidales]

Protein Classification

6-pyruvoyl trahydropterin synthase family protein( domain architecture ID 10002285)

6-pyruvoyl tetrahydropterin synthase (PTPS) family protein similar to 6-carboxy-5,6,7,8-tetrahydropterin synthase that catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde, and dihydroneopterin monophosphate aldolase that catalyzes the conversion of 7,8-dihydroneopterin monophosphate (H2NMP) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD)

CATH:  3.30.479.10
EC:  4.1.2.-
Gene Ontology:  GO:0016829|GO:0046872
PubMed:  10737935|21999246
SCOP:  4001717

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
QueD COG0720
6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; ...
 1-110 1.03e-39

6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; 6-pyruvoyl-tetrahydropterin synthase is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440484  Cd Length: 123  Bit Score: 128.39  E-value: 1.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344   1 MYTVIKRMEISASHSLKlSYRSKCENLHGHNWIITVYCRSEVLNEDGMVVDFTHIKE---TVMGRLDHRNLNEVVSF--- 74
Cdd:COG0720    1 MYRITKEFRFSAAHRLP-GHDGKCGRLHGHNYRVEVTVEGEELDETGMVVDFGDLKAalkEVIDRLDHRFLNELPDLegl 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 492422344  75 NPTAENIARWVCEQI-------PTCFKVEVRESEGNTVIYEKD 110
Cdd:COG0720   80 NPTAENLARWIWDRLaprlpggVRLLRVRVYETPTNWAEYEGE 122
 
Name Accession Description Interval E-value
QueD COG0720
6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; ...
 1-110 1.03e-39

6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; 6-pyruvoyl-tetrahydropterin synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440484  Cd Length: 123  Bit Score: 128.39  E-value: 1.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344   1 MYTVIKRMEISASHSLKlSYRSKCENLHGHNWIITVYCRSEVLNEDGMVVDFTHIKE---TVMGRLDHRNLNEVVSF--- 74
Cdd:COG0720    1 MYRITKEFRFSAAHRLP-GHDGKCGRLHGHNYRVEVTVEGEELDETGMVVDFGDLKAalkEVIDRLDHRFLNELPDLegl 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 492422344  75 NPTAENIARWVCEQI-------PTCFKVEVRESEGNTVIYEKD 110
Cdd:COG0720   80 NPTAENLARWIWDRLaprlpggVRLLRVRVYETPTNWAEYEGE 122
PTPS pfam01242
6-pyruvoyl tetrahydropterin synthase; 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the ...
 3-108 1.71e-38

6-pyruvoyl tetrahydropterin synthase; 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP. The functional enzyme is a hexamer of identical subunits.


Pssm-ID: 460129  Cd Length: 121  Bit Score: 125.00  E-value: 1.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344    3 TVIKRMEISASHSLKlSYRSKCENLHGHNWIITVYCRSEVLNEDGMVVDFTHIKE---TVMGRLDHRNLNEVVSF---NP 76
Cdd:pfam01242   1 EITKEFRFDAAHRLP-DYPGKCSNLHGHNYRVEVTVRGEELDETGMVVDFGELKKavkEVLDRLDHRFLNDDPEFetlNP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 492422344   77 TAENIARWVCEQI--------PTCFKVEVRESEGNTVIYE 108
Cdd:pfam01242  80 TAENLARYIFERLkprlsgggVRLARVRVWETPTSWAEYR 119
queuosine_QueD TIGR03367
queuosine biosynthesis protein QueD; Members of this protein family, closely related to ...
 6-89 2.88e-29

queuosine biosynthesis protein QueD; Members of this protein family, closely related to eukaryotic 6-pyruvoyl tetrahydrobiopterin synthase enzymes, are the QueD protein of queuosine biosynthesis. Queuosine is a hypermodified base in the wobble position of tRNAs for Tyr, His, Asp, and Asn in many species. This modification, although widespread, appears not to be important for viability. The queuosine precursor made by this enzyme may be converted instead to archeaosine as in some Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274547  Cd Length: 89  Bit Score: 100.74  E-value: 2.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344    6 KRMEISASHSLkLSYRSKCENLHGHNWIITVYCRSEVLNEDGMVVDFTHIKETVM---GRLDHRNLNEVVSF-NPTAENI 81
Cdd:TIGR03367   3 KEFTFDAAHRL-PGYPGKCARLHGHTYKVEVTVSGEVLDEAGMVMDFSDLKAIVKevvDRLDHALLNDVLGLeNPTAENL 81


                  ....*...
gi 492422344   82 ARWVCEQI 89
Cdd:TIGR03367  82 ARWIYDRL 89
PTPS cd00470
6-pyruvoyl tetrahydropterin synthase (PTPS). Folate derivatives are essential cofactors in the ...
 3-107 5.69e-16

6-pyruvoyl tetrahydropterin synthase (PTPS). Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids, as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is PTPS which catalyzes the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin. The functional enzyme is a hexamer of identical subunits.


Pssm-ID: 238264  Cd Length: 135  Bit Score: 68.42  E-value: 5.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344   3 TVIKRMEISASH---SLKLSYRS------KCEN--LHGHNWIITVYCRSEVLNEDGMVVDFTHIK----ETVMGRLDHRN 67
Cdd:cd00470    3 TLTRRFSFSACHrlhSPPLSDEEnlevfgKCNNpnGHGHNYKVEVTVRGEIDPVTGMVMNLTDLKkaieEAIMKPLDHKN 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 492422344  68 LNEVVSF----NPTAENIARWVCEQI------PTCFKVEVRESEGNTVIY 107
Cdd:cd00470   83 LDDDVPYfadvVSTTENLAVYIWDNLqkvlpvGLLYEVKVHETDKNIVVY 132
 
Name Accession Description Interval E-value
QueD COG0720
6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; ...
 1-110 1.03e-39

6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; 6-pyruvoyl-tetrahydropterin synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440484  Cd Length: 123  Bit Score: 128.39  E-value: 1.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344   1 MYTVIKRMEISASHSLKlSYRSKCENLHGHNWIITVYCRSEVLNEDGMVVDFTHIKE---TVMGRLDHRNLNEVVSF--- 74
Cdd:COG0720    1 MYRITKEFRFSAAHRLP-GHDGKCGRLHGHNYRVEVTVEGEELDETGMVVDFGDLKAalkEVIDRLDHRFLNELPDLegl 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 492422344  75 NPTAENIARWVCEQI-------PTCFKVEVRESEGNTVIYEKD 110
Cdd:COG0720   80 NPTAENLARWIWDRLaprlpggVRLLRVRVYETPTNWAEYEGE 122
PTPS pfam01242
6-pyruvoyl tetrahydropterin synthase; 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the ...
 3-108 1.71e-38

6-pyruvoyl tetrahydropterin synthase; 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP. The functional enzyme is a hexamer of identical subunits.


Pssm-ID: 460129  Cd Length: 121  Bit Score: 125.00  E-value: 1.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344    3 TVIKRMEISASHSLKlSYRSKCENLHGHNWIITVYCRSEVLNEDGMVVDFTHIKE---TVMGRLDHRNLNEVVSF---NP 76
Cdd:pfam01242   1 EITKEFRFDAAHRLP-DYPGKCSNLHGHNYRVEVTVRGEELDETGMVVDFGELKKavkEVLDRLDHRFLNDDPEFetlNP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 492422344   77 TAENIARWVCEQI--------PTCFKVEVRESEGNTVIYE 108
Cdd:pfam01242  80 TAENLARYIFERLkprlsgggVRLARVRVWETPTSWAEYR 119
queuosine_QueD TIGR03367
queuosine biosynthesis protein QueD; Members of this protein family, closely related to ...
 6-89 2.88e-29

queuosine biosynthesis protein QueD; Members of this protein family, closely related to eukaryotic 6-pyruvoyl tetrahydrobiopterin synthase enzymes, are the QueD protein of queuosine biosynthesis. Queuosine is a hypermodified base in the wobble position of tRNAs for Tyr, His, Asp, and Asn in many species. This modification, although widespread, appears not to be important for viability. The queuosine precursor made by this enzyme may be converted instead to archeaosine as in some Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274547  Cd Length: 89  Bit Score: 100.74  E-value: 2.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344    6 KRMEISASHSLkLSYRSKCENLHGHNWIITVYCRSEVLNEDGMVVDFTHIKETVM---GRLDHRNLNEVVSF-NPTAENI 81
Cdd:TIGR03367   3 KEFTFDAAHRL-PGYPGKCARLHGHTYKVEVTVSGEVLDEAGMVMDFSDLKAIVKevvDRLDHALLNDVLGLeNPTAENL 81


                  ....*...
gi 492422344   82 ARWVCEQI 89
Cdd:TIGR03367  82 ARWIYDRL 89
6PTHBS TIGR00039
6-pyruvoyl tetrahydropterin synthase/QueD family protein; This model has been downgraded from ...
 1-108 8.75e-21

6-pyruvoyl tetrahydropterin synthase/QueD family protein; This model has been downgraded from hypothetical_equivalog to subfamily. The animal enzymes are known to be 6-pyruvoyl tetrahydropterin synthase. The function of the bacterial branch of the sequence lineage had been thought to be the same, but many are now taken to be QueD, and enzyme of queuosine biosynthesis. Queuosine is a hypermodified base in the wobble position of some tRNAs in most species. A new model is built to be the QueD equivalog model. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272868  Cd Length: 124  Bit Score: 80.10  E-value: 8.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344    1 MYTVIKRMEISASHSLKlSYRSKCENLHGHNWIITVYCRSEVLNEDGMVVDFT----HIKETVMGRLDHRNLNEVVSF-- 74
Cdd:TIGR00039   1 MFGIHKEFSFSAAHRLP-GHEGKCGNLHGHSYKVDVEVSGERDPKTGMVMDFSdlkkIVKEVIDEPLDHKLLNDDVNYle 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 492422344   75 NPTAENIARWVCEQ-------IPTCFKVEVRESEGNTVIYE 108
Cdd:TIGR00039  80 NPTSENVAVYIFDNlkeylipVENLVKVKEEETPAEIRIYR 120
PTPS cd00470
6-pyruvoyl tetrahydropterin synthase (PTPS). Folate derivatives are essential cofactors in the ...
 3-107 5.69e-16

6-pyruvoyl tetrahydropterin synthase (PTPS). Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids, as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is PTPS which catalyzes the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin. The functional enzyme is a hexamer of identical subunits.


Pssm-ID: 238264  Cd Length: 135  Bit Score: 68.42  E-value: 5.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422344   3 TVIKRMEISASH---SLKLSYRS------KCEN--LHGHNWIITVYCRSEVLNEDGMVVDFTHIK----ETVMGRLDHRN 67
Cdd:cd00470    3 TLTRRFSFSACHrlhSPPLSDEEnlevfgKCNNpnGHGHNYKVEVTVRGEIDPVTGMVMNLTDLKkaieEAIMKPLDHKN 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 492422344  68 LNEVVSF----NPTAENIARWVCEQI------PTCFKVEVRESEGNTVIY 107
Cdd:cd00470   83 LDDDVPYfadvVSTTENLAVYIWDNLqkvlpvGLLYEVKVHETDKNIVVY 132
 
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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