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Conserved domains on  [gi|4239875|dbj|BAA74727|]
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Glutamine:fructose-6-phosphate amidotransferase 2, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02981 super family cl33615
glucosamine:fructose-6-phosphate aminotransferase
 1-33 4.43e-13

glucosamine:fructose-6-phosphate aminotransferase


The actual alignment was detected with superfamily member PLN02981:

Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 59.76  E-value: 4.43e-13
                         10        20        30
                 ....*....|....*....|....*....|...
gi 4239875     1 IFAYMNYRVPKTRKEIFETLIRGLQRLEYRGYD 33
Cdd:PLN02981   4 IFAYLNYNVPRERRFILEVLFNGLRRLEYRGYD 36
 
Name Accession Description Interval E-value
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 1-33 4.43e-13

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 59.76  E-value: 4.43e-13
                         10        20        30
                 ....*....|....*....|....*....|...
gi 4239875     1 IFAYMNYRVPKTRKEIFETLIRGLQRLEYRGYD 33
Cdd:PLN02981   4 IFAYLNYNVPRERRFILEVLFNGLRRLEYRGYD 36
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 1-33 5.13e-10

Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.


Pssm-ID: 238366 [Multi-domain]  Cd Length: 215  Bit Score: 50.52  E-value: 5.13e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 4239875    1 IFAYMNYRvpktrkEIFETLIRGLQRLEYRGYD 33
Cdd:cd00714   3 IVGYIGKR------EAVDILLEGLKRLEYRGYD 29
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 13-33 3.55e-06

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 40.00  E-value: 3.55e-06
                        10        20
                ....*....|....*....|.
gi 4239875   13 RKEIFETLIRGLQRLEYRGYD 33
Cdd:COG0449  10 KRDAAPILLEGLKRLEYRGYD 30
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 20-33 6.41e-05

glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 273462 [Multi-domain]  Cd Length: 607  Bit Score: 36.85  E-value: 6.41e-05
                          10
                  ....*....|....
gi 4239875     20 LIRGLQRLEYRGYD 33
Cdd:TIGR01135  16 LLEGLKRLEYRGYD 29
 
Name Accession Description Interval E-value
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 1-33 4.43e-13

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 59.76  E-value: 4.43e-13
                         10        20        30
                 ....*....|....*....|....*....|...
gi 4239875     1 IFAYMNYRVPKTRKEIFETLIRGLQRLEYRGYD 33
Cdd:PLN02981   4 IFAYLNYNVPRERRFILEVLFNGLRRLEYRGYD 36
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 1-33 8.15e-12

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 56.04  E-value: 8.15e-12
                         10        20        30
                 ....*....|....*....|....*....|...
gi 4239875     1 IFAYMNYRVPKTRKEIFETLIRGLQRLEYRGYD 33
Cdd:PTZ00394   4 IFGYANHNVPRTVEQILNVLLDGIQKVEYRGYD 36
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 1-33 5.13e-10

Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.


Pssm-ID: 238366 [Multi-domain]  Cd Length: 215  Bit Score: 50.52  E-value: 5.13e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 4239875    1 IFAYMNYRvpktrkEIFETLIRGLQRLEYRGYD 33
Cdd:cd00714   3 IVGYIGKR------EAVDILLEGLKRLEYRGYD 29
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 13-33 3.55e-06

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 40.00  E-value: 3.55e-06
                        10        20
                ....*....|....*....|.
gi 4239875   13 RKEIFETLIRGLQRLEYRGYD 33
Cdd:COG0449  10 KRDAAPILLEGLKRLEYRGYD 30
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
13-33 4.36e-06

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 40.03  E-value: 4.36e-06
                         10        20
                 ....*....|....*....|.
gi 4239875    13 RKEIFETLIRGLQRLEYRGYD 33
Cdd:PRK00331  10 QRNAAEILLEGLKRLEYRGYD 30
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 20-33 6.41e-05

glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 273462 [Multi-domain]  Cd Length: 607  Bit Score: 36.85  E-value: 6.41e-05
                          10
                  ....*....|....
gi 4239875     20 LIRGLQRLEYRGYD 33
Cdd:TIGR01135  16 LLEGLKRLEYRGYD 29
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 1-33 1.64e-03

Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.


Pssm-ID: 238212 [Multi-domain]  Cd Length: 220  Bit Score: 32.81  E-value: 1.64e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 4239875    1 IFAYMNYRVPKTRKEIfeTLIRGLQRLEYRGYD 33
Cdd:cd00352   3 IFGIVGADGAASLLLL--LLLRGLAALEHRGPD 33
 
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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