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Conserved domains on  [gi|491150629|ref|WP_005009024|]
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6-carboxytetrahydropterin synthase [Acinetobacter bouvetii]

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]; ...
 1-148 9.17e-29

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: 103.74  E-value: 9.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629   1 MLIRKLFKFENAHIVRNCtSDRCKRsIHGHSYKVELLLKASKLDHGQMVYDFGLLKGVIKDLYDSFDHAICFWQQDNAGy 80
Cdd:COG0720    2 YRITKEFRFSAAHRLPGH-DGKCGR-LHGHNYRVEVTVEGEELDETGMVVDFGDLKAALKEVIDRLDHRFLNELPDLEG- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491150629  81 ieacknfsarwvslpVSPSAEQFSRIFFYLAQQVLastetqngEGDVEVYSVIVHETDTGYAQSFAED 148
Cdd:COG0720   79 ---------------LNPTAENLARWIWDRLAPRL--------PGGVRLLRVRVYETPTNWAEYEGEL 123
 
Name Accession Description Interval E-value
QueD COG0720
6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; ...
 1-148 9.17e-29

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: 103.74  E-value: 9.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629   1 MLIRKLFKFENAHIVRNCtSDRCKRsIHGHSYKVELLLKASKLDHGQMVYDFGLLKGVIKDLYDSFDHAICFWQQDNAGy 80
Cdd:COG0720    2 YRITKEFRFSAAHRLPGH-DGKCGR-LHGHNYRVEVTVEGEELDETGMVVDFGDLKAALKEVIDRLDHRFLNELPDLEG- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491150629  81 ieacknfsarwvslpVSPSAEQFSRIFFYLAQQVLastetqngEGDVEVYSVIVHETDTGYAQSFAED 148
Cdd:COG0720   79 ---------------LNPTAENLARWIWDRLAPRL--------PGGVRLLRVRVYETPTNWAEYEGEL 123
PTPS pfam01242
6-pyruvoyl tetrahydropterin synthase; 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the ...
 3-142 1.14e-23

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: 90.72  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629    3 IRKLFKFENAHIVRNcTSDRCKRsIHGHSYKVELLLKASKLDHGQMVYDFGLLKGVIKDLYDSFDHAIcfwQQDNAGYIE 82
Cdd:pfam01242   2 ITKEFRFDAAHRLPD-YPGKCSN-LHGHNYRVEVTVRGEELDETGMVVDFGELKKAVKEVLDRLDHRF---LNDDPEFET 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629   83 ACknfsarwvslpvsPSAEQFSRIFFYLAQQVLastetqnGEGDVEVYSVIVHETDTGYA 142
Cdd:pfam01242  77 LN-------------PTAENLARYIFERLKPRL-------SGGGVRLARVRVWETPTSWA 116
queuosine_QueD TIGR03367
queuosine biosynthesis protein QueD; Members of this protein family, closely related to ...
 3-108 3.44e-19

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: 78.01  E-value: 3.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629    3 IRKLFKFENAHIVRNCTSdRCKRsIHGHSYKVELLLKASKLDHGQMVYDFGLLKGVIKDLYDSFDHAICFwqqdnagYIE 82
Cdd:TIGR03367   1 ITKEFTFDAAHRLPGYPG-KCAR-LHGHTYKVEVTVSGEVLDEAGMVMDFSDLKAIVKEVVDRLDHALLN-------DVL 71

                          90       100
                  ....*....|....*....|....*.
gi 491150629   83 ACKNfsarwvslpvsPSAEQFSRIFF 108
Cdd:TIGR03367  72 GLEN-----------PTAENLARWIY 86
 
Name Accession Description Interval E-value
QueD COG0720
6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]; ...
 1-148 9.17e-29

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: 103.74  E-value: 9.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629   1 MLIRKLFKFENAHIVRNCtSDRCKRsIHGHSYKVELLLKASKLDHGQMVYDFGLLKGVIKDLYDSFDHAICFWQQDNAGy 80
Cdd:COG0720    2 YRITKEFRFSAAHRLPGH-DGKCGR-LHGHNYRVEVTVEGEELDETGMVVDFGDLKAALKEVIDRLDHRFLNELPDLEG- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491150629  81 ieacknfsarwvslpVSPSAEQFSRIFFYLAQQVLastetqngEGDVEVYSVIVHETDTGYAQSFAED 148
Cdd:COG0720   79 ---------------LNPTAENLARWIWDRLAPRL--------PGGVRLLRVRVYETPTNWAEYEGEL 123
PTPS pfam01242
6-pyruvoyl tetrahydropterin synthase; 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the ...
 3-142 1.14e-23

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: 90.72  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629    3 IRKLFKFENAHIVRNcTSDRCKRsIHGHSYKVELLLKASKLDHGQMVYDFGLLKGVIKDLYDSFDHAIcfwQQDNAGYIE 82
Cdd:pfam01242   2 ITKEFRFDAAHRLPD-YPGKCSN-LHGHNYRVEVTVRGEELDETGMVVDFGELKKAVKEVLDRLDHRF---LNDDPEFET 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629   83 ACknfsarwvslpvsPSAEQFSRIFFYLAQQVLastetqnGEGDVEVYSVIVHETDTGYA 142
Cdd:pfam01242  77 LN-------------PTAENLARYIFERLKPRL-------SGGGVRLARVRVWETPTSWA 116
queuosine_QueD TIGR03367
queuosine biosynthesis protein QueD; Members of this protein family, closely related to ...
 3-108 3.44e-19

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: 78.01  E-value: 3.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629    3 IRKLFKFENAHIVRNCTSdRCKRsIHGHSYKVELLLKASKLDHGQMVYDFGLLKGVIKDLYDSFDHAICFwqqdnagYIE 82
Cdd:TIGR03367   1 ITKEFTFDAAHRLPGYPG-KCAR-LHGHTYKVEVTVSGEVLDEAGMVMDFSDLKAIVKEVVDRLDHALLN-------DVL 71

                          90       100
                  ....*....|....*....|....*.
gi 491150629   83 ACKNfsarwvslpvsPSAEQFSRIFF 108
Cdd:TIGR03367  72 GLEN-----------PTAENLARWIY 86
6PTHBS TIGR00039
6-pyruvoyl tetrahydropterin synthase/QueD family protein; This model has been downgraded from ...
 1-69 1.26e-08

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: 51.21  E-value: 1.26e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150629    1 MLIRKLFKFENAHIVRNCTSdRCKRsIHGHSYKVELLLKASKLDHGQMVYDFGLLKGVIKDLYD-SFDHA 69
Cdd:TIGR00039   2 FGIHKEFSFSAAHRLPGHEG-KCGN-LHGHSYKVDVEVSGERDPKTGMVMDFSDLKKIVKEVIDePLDHK 69
 
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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