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Conserved domains on  [gi|950381|gb|AAB59592|]
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galactose-1-phosphate uridyl transferase, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11720 super family cl29677
UDP-glucose--hexose-1-phosphate uridylyltransferase;
1-41 2.16e-12

UDP-glucose--hexose-1-phosphate uridylyltransferase;


The actual alignment was detected with superfamily member PRK11720:

Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 58.38  E-value: 2.16e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 950381      1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:PRK11720 169 IWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADG 209
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
1-41 2.16e-12

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 58.38  E-value: 2.16e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 950381      1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:PRK11720 169 IWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADG 209
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
 1-41 2.14e-09

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 49.61  E-value: 2.14e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 950381     1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:cd00608 159 IWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESK 199
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
 1-41 1.06e-06

galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]


Pssm-ID: 129313 [Multi-domain]  Cd Length: 347  Bit Score: 42.26  E-value: 1.06e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 950381       1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:TIGR00209 169 IWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADK 209
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
1-38 2.20e-06

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 41.36  E-value: 2.20e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 950381     1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQEL 38
Cdd:COG1085 165 IIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQEL 202
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
 14-41 1.36e-04

Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 397044 [Multi-domain]  Cd Length: 166  Bit Score: 35.92  E-value: 1.36e-04
                          10        20
                  ....*....|....*....|....*...
gi 950381      14 EERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEK 28
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
1-41 2.16e-12

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 58.38  E-value: 2.16e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 950381      1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:PRK11720 169 IWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADG 209
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
 1-41 2.14e-09

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 49.61  E-value: 2.14e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 950381     1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:cd00608 159 IWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESK 199
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
 1-41 1.06e-06

galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]


Pssm-ID: 129313 [Multi-domain]  Cd Length: 347  Bit Score: 42.26  E-value: 1.06e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 950381       1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:TIGR00209 169 IWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADK 209
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
1-38 2.20e-06

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 41.36  E-value: 2.20e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 950381     1 VWASSFLPDIAQHEERSQQAYKSQHGEPLLMEYSRQEL 38
Cdd:COG1085 165 IIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQEL 202
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
 14-41 1.36e-04

Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 397044 [Multi-domain]  Cd Length: 166  Bit Score: 35.92  E-value: 1.36e-04
                          10        20
                  ....*....|....*....|....*...
gi 950381      14 EERSQQAYKSQHGEPLLMEYSRQELLRK 41
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEK 28
 
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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