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Conserved domains on  [gi|347520527|gb|EGY27660|]
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queuosine biosynthesis protein QueD [Desulfovibrio sp. A2]

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]; ...
 6-125 5.07e-49

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: 152.66  E-value: 5.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527   6 WRLTVRSEFCASHALRHYEGKCESMHGHNFAVEMVAEGDRLtGDTEIVLDFKELKRELNAVLDTLDHKNLNDVPPFDAIN 85
Cdd:COG0720    2 YRITKEFRFSAAHRLPGHDGKCGRLHGHNYRVEVTVEGEEL-DETGMVVDFGDLKAALKEVIDRLDHRFLNELPDLEGLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 347520527  86 PSSENLSRHIWQLLAPRLaPHGVRLHAVTVSEKAAQSATY 125
Cdd:COG0720   81 PTAENLARWIWDRLAPRL-PGGVRLLRVRVYETPTNWAEY 119
 
Name Accession Description Interval E-value
QueD COG0720
6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; ...
 6-125 5.07e-49

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: 152.66  E-value: 5.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527   6 WRLTVRSEFCASHALRHYEGKCESMHGHNFAVEMVAEGDRLtGDTEIVLDFKELKRELNAVLDTLDHKNLNDVPPFDAIN 85
Cdd:COG0720    2 YRITKEFRFSAAHRLPGHDGKCGRLHGHNYRVEVTVEGEEL-DETGMVVDFGDLKAALKEVIDRLDHRFLNELPDLEGLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 347520527  86 PSSENLSRHIWQLLAPRLaPHGVRLHAVTVSEKAAQSATY 125
Cdd:COG0720   81 PTAENLARWIWDRLAPRL-PGGVRLLRVRVYETPTNWAEY 119
PTPS pfam01242
6-pyruvoyl tetrahydropterin synthase; 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the ...
 7-127 8.24e-48

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: 149.65  E-value: 8.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527    7 RLTVRSEFCASHALRHYEGKCESMHGHNFAVEMVAEGDRLtGDTEIVLDFKELKRELNAVLDTLDHKNLNDVPPFDAINP 86
Cdd:pfam01242   1 EITKEFRFDAAHRLPDYPGKCSNLHGHNYRVEVTVRGEEL-DETGMVVDFGELKKAVKEVLDRLDHRFLNDDPEFETLNP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 347520527   87 SSENLSRHIWQLLAPRLAPHGVRLHAVTVSEKAAQSATYME 127
Cdd:pfam01242  80 TAENLARYIFERLKPRLSGGGVRLARVRVWETPTSWAEYRG 120
queuosine_QueD TIGR03367
queuosine biosynthesis protein QueD; Members of this protein family, closely related to ...
 8-99 6.66e-30

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: 103.05  E-value: 6.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527    8 LTVRSEFCASHALRHYEGKCESMHGHNFAVEMVAEGDRLtGDTEIVLDFKELKRELNAVLDTLDHKNLNDVPPFDaiNPS 87
Cdd:TIGR03367   1 ITKEFTFDAAHRLPGYPGKCARLHGHTYKVEVTVSGEVL-DEAGMVMDFSDLKAIVKEVVDRLDHALLNDVLGLE--NPT 77

                          90
                  ....*....|..
gi 347520527   88 SENLSRHIWQLL 99
Cdd:TIGR03367  78 AENLARWIYDRL 89
PTPS cd00470
6-pyruvoyl tetrahydropterin synthase (PTPS). Folate derivatives are essential cofactors in the ...
 7-111 5.49e-17

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: 71.50  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527   7 RLTVRSEFCASHALRHYE----------GKCES--MHGHNFAVEMVAEG--DRLTGdteIVLDFKELKREL-NAVLDTLD 71
Cdd:cd00470    3 TLTRRFSFSACHRLHSPPlsdeenlevfGKCNNpnGHGHNYKVEVTVRGeiDPVTG---MVMNLTDLKKAIeEAIMKPLD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 347520527  72 HKNLNDVPPFDA-INPSSENLSRHIW---QLLAPRLAPHGVRLH 111
Cdd:cd00470   80 HKNLDDDVPYFAdVVSTTENLAVYIWdnlQKVLPVGLLYEVKVH 123
 
Name Accession Description Interval E-value
QueD COG0720
6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; ...
 6-125 5.07e-49

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: 152.66  E-value: 5.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527   6 WRLTVRSEFCASHALRHYEGKCESMHGHNFAVEMVAEGDRLtGDTEIVLDFKELKRELNAVLDTLDHKNLNDVPPFDAIN 85
Cdd:COG0720    2 YRITKEFRFSAAHRLPGHDGKCGRLHGHNYRVEVTVEGEEL-DETGMVVDFGDLKAALKEVIDRLDHRFLNELPDLEGLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 347520527  86 PSSENLSRHIWQLLAPRLaPHGVRLHAVTVSEKAAQSATY 125
Cdd:COG0720   81 PTAENLARWIWDRLAPRL-PGGVRLLRVRVYETPTNWAEY 119
PTPS pfam01242
6-pyruvoyl tetrahydropterin synthase; 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the ...
 7-127 8.24e-48

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: 149.65  E-value: 8.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527    7 RLTVRSEFCASHALRHYEGKCESMHGHNFAVEMVAEGDRLtGDTEIVLDFKELKRELNAVLDTLDHKNLNDVPPFDAINP 86
Cdd:pfam01242   1 EITKEFRFDAAHRLPDYPGKCSNLHGHNYRVEVTVRGEEL-DETGMVVDFGELKKAVKEVLDRLDHRFLNDDPEFETLNP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 347520527   87 SSENLSRHIWQLLAPRLAPHGVRLHAVTVSEKAAQSATYME 127
Cdd:pfam01242  80 TAENLARYIFERLKPRLSGGGVRLARVRVWETPTSWAEYRG 120
queuosine_QueD TIGR03367
queuosine biosynthesis protein QueD; Members of this protein family, closely related to ...
 8-99 6.66e-30

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: 103.05  E-value: 6.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527    8 LTVRSEFCASHALRHYEGKCESMHGHNFAVEMVAEGDRLtGDTEIVLDFKELKRELNAVLDTLDHKNLNDVPPFDaiNPS 87
Cdd:TIGR03367   1 ITKEFTFDAAHRLPGYPGKCARLHGHTYKVEVTVSGEVL-DEAGMVMDFSDLKAIVKEVVDRLDHALLNDVLGLE--NPT 77

                          90
                  ....*....|..
gi 347520527   88 SENLSRHIWQLL 99
Cdd:TIGR03367  78 AENLARWIYDRL 89
6PTHBS TIGR00039
6-pyruvoyl tetrahydropterin synthase/QueD family protein; This model has been downgraded from ...
 5-125 7.27e-22

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: 83.95  E-value: 7.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527    5 IWRLTVRSEFCASHALRHYEGKCESMHGHNFAVEMVAEGDRLtGDTEIVLDFKELKRELNAVLD-TLDHKNLNDVPPFDa 83
Cdd:TIGR00039   1 MFGIHKEFSFSAAHRLPGHEGKCGNLHGHSYKVDVEVSGERD-PKTGMVMDFSDLKKIVKEVIDePLDHKLLNDDVNYL- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 347520527   84 INPSSENLSRHIWQLLAPRLAPhGVRLHAVTVSEKAAQSATY 125
Cdd:TIGR00039  79 ENPTSENVAVYIFDNLKEYLIP-VENLVKVKEEETPAEIRIY 119
PTPS cd00470
6-pyruvoyl tetrahydropterin synthase (PTPS). Folate derivatives are essential cofactors in the ...
 7-111 5.49e-17

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: 71.50  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527   7 RLTVRSEFCASHALRHYE----------GKCES--MHGHNFAVEMVAEG--DRLTGdteIVLDFKELKREL-NAVLDTLD 71
Cdd:cd00470    3 TLTRRFSFSACHRLHSPPlsdeenlevfGKCNNpnGHGHNYKVEVTVRGeiDPVTG---MVMNLTDLKKAIeEAIMKPLD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 347520527  72 HKNLNDVPPFDA-INPSSENLSRHIW---QLLAPRLAPHGVRLH 111
Cdd:cd00470   80 HKNLDDDVPYFAdVVSTTENLAVYIWdnlQKVLPVGLLYEVKVH 123
6_pyr_pter_rel TIGR03112
6-pyruvoyl tetrahydropterin synthase-related domain; Members of this family are small proteins, ...
 16-122 4.50e-11

6-pyruvoyl tetrahydropterin synthase-related domain; Members of this family are small proteins, or small domains of larger proteins, that occur in certain Firmicutes in the same regions as members of families TIGR03110 and TIGR03111. Members of TIGR03110 resemble exosortase, a proposed protein sorting transpeptidase (see TIGR02602). TIGR03111 represents a small clade among the group 2 glycosyltransferases. Members of the current protein family resemble eukaryotic known and prokaryotic predicted 6-pyruvoyl tetrahydropterin synthases.


Pssm-ID: 132156  Cd Length: 113  Bit Score: 55.84  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347520527   16 ASHALRhYEGKCESMHGHNFAVEMVAegdrLTGDTEIVLdFKELKRELNAVLDTLDHKNLNDVPPFDAINPSSENLSRHI 95
Cdd:TIGR03112   9 ASHSII-INGVRGNKHPHTWEITIFV----IKKEDKFIL-FNDVEKKVEKYLKPYQNKYLNDLEPFDKINPTLENIGDYF 82

                          90       100
                  ....*....|....*....|....*..
gi 347520527   96 WQLLAPRLAPHGVRLHAVTVSEKAAQS 122
Cdd:TIGR03112  83 FDEIKKLLKEKGWKLHSIEISETPTRT 109
 
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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