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Conserved domains on  [gi|768021794|ref|XP_011528064|]
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pyridoxal kinase isoform X6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
105-141 4.62e-06

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


The actual alignment was detected with superfamily member TIGR00687:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 287  Bit Score: 45.21  E-value: 4.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 768021794  105 ALTSWApVRGEVRKKT---PSEVLGFEIDAVNSVQFSNHT 141
Cdd:TIGR00687   6 SIQSHV-VYGHVGNRAatfPLQRLGFEVWAVNTVQFSNHT 44
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
125-172 9.08e-05

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


The actual alignment was detected with superfamily member cd01173:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 254  Bit Score: 41.42  E-value: 9.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 768021794 125 LGFEIDAVNSVQFSNHTaltpapQCGTGFGDGAPT-EVSRLKEAIRALG 172
Cdd:cd01173   26 LGWDVDALPTVQFSNHT------GYGTWTGFVLSAeELEDLLEGLEALG 68
 
Name Accession Description Interval E-value
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
105-141 4.62e-06

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 45.21  E-value: 4.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 768021794  105 ALTSWApVRGEVRKKT---PSEVLGFEIDAVNSVQFSNHT 141
Cdd:TIGR00687   6 SIQSHV-VYGHVGNRAatfPLQRLGFEVWAVNTVQFSNHT 44
PLN02978 PLN02978
pyridoxal kinase
112-141 7.06e-06

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 44.73  E-value: 7.06e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 768021794 112 VRGEVRKKT---PSEVLGFEIDAVNSVQFSNHT 141
Cdd:PLN02978  25 VHGYVGNKSavfPLQLLGFDVDPINSVQFSNHT 57
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
125-172 9.08e-05

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 41.42  E-value: 9.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 768021794 125 LGFEIDAVNSVQFSNHTaltpapQCGTGFGDGAPT-EVSRLKEAIRALG 172
Cdd:cd01173   26 LGWDVDALPTVQFSNHT------GYGTWTGFVLSAeELEDLLEGLEALG 68
 
Name Accession Description Interval E-value
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
105-141 4.62e-06

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 45.21  E-value: 4.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 768021794  105 ALTSWApVRGEVRKKT---PSEVLGFEIDAVNSVQFSNHT 141
Cdd:TIGR00687   6 SIQSHV-VYGHVGNRAatfPLQRLGFEVWAVNTVQFSNHT 44
PLN02978 PLN02978
pyridoxal kinase
112-141 7.06e-06

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 44.73  E-value: 7.06e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 768021794 112 VRGEVRKKT---PSEVLGFEIDAVNSVQFSNHT 141
Cdd:PLN02978  25 VHGYVGNKSavfPLQLLGFDVDPINSVQFSNHT 57
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
121-142 5.35e-05

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 42.38  E-value: 5.35e-05
                         10        20
                 ....*....|....*....|..
gi 768021794 121 PSEVLGFEIDAVNSVQFSNHTA 142
Cdd:PTZ00344  27 PLQLLGFDVDFVNTVQLSNHTG 48
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
125-172 9.08e-05

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 41.42  E-value: 9.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 768021794 125 LGFEIDAVNSVQFSNHTaltpapQCGTGFGDGAPT-EVSRLKEAIRALG 172
Cdd:cd01173   26 LGWDVDALPTVQFSNHT------GYGTWTGFVLSAeELEDLLEGLEALG 68
 
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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