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Conserved domains on  [gi|9887335|gb|AAG01855|]
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formiminotransferase cyclodeaminase form E [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FtcD super family cl46938
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
 1-136 1.93e-79

glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]


The actual alignment was detected with superfamily member TIGR02024:

Pssm-ID: 131079 [Multi-domain]  Cd Length: 298  Bit Score: 237.35  E-value: 1.93e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9887335      1 MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQG 80
Cdd:TIGR02024   1 MMKLVECVPNFSEGRNKEVIEKIVDAIIKTDNVKLLDVDMDPDHNRSVITFVGEPECVVNAALKLAKKAAELIDMRNHKG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 9887335     81 EHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPGLTAGLSCSLPVRR 136
Cdd:TIGR02024  81 EHPRMGAADVIPFIPVRNVTMEECVELAKEFGKRLGEELGVPVYLYEEAATRPERQ 136
 
Name Accession Description Interval E-value
FtcD TIGR02024
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
 1-136 1.93e-79

glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131079 [Multi-domain]  Cd Length: 298  Bit Score: 237.35  E-value: 1.93e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9887335      1 MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQG 80
Cdd:TIGR02024   1 MMKLVECVPNFSEGRNKEVIEKIVDAIIKTDNVKLLDVDMDPDHNRSVITFVGEPECVVNAALKLAKKAAELIDMRNHKG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 9887335     81 EHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPGLTAGLSCSLPVRR 136
Cdd:TIGR02024  81 EHPRMGAADVIPFIPVRNVTMEECVELAKEFGKRLGEELGVPVYLYEEAATRPERQ 136
FTCD_N pfam07837
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
 4-137 1.63e-76

Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.


Pssm-ID: 462283  Cd Length: 176  Bit Score: 225.43  E-value: 1.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9887335      4 LVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQGEHP 83
Cdd:pfam07837   1 LVECVPNFSEGRDKEVIEAIARAARSVPGVKLLDVFSDADHNRTVVTLVGEPEAVVEAALAAAKKAFELIDMRKHKGEHP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 9887335     84 RMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPGLTAGLSCSLPVRRG 137
Cdd:pfam07837  81 RMGAVDVIPFVPLRGVTMEECVELAKELAKRIGEELGVPVYLYEAAATRPERRN 134
GluFT COG3643
Glutamate formiminotransferase [Amino acid transport and metabolism];
1-136 2.23e-74

Glutamate formiminotransferase [Amino acid transport and metabolism];


Pssm-ID: 442860 [Multi-domain]  Cd Length: 303  Bit Score: 224.27  E-value: 2.23e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9887335    1 MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQG 80
Cdd:COG3643   1 MMKIVECVPNFSEGRDKEVIEAIVDAIRSVEGVKLLDYSPDADHNRTVVTFVGEPEAVKEAAFNAAKKAAELIDMTKHKG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 9887335   81 EHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPGLTAGLSCSLPVRR 136
Cdd:COG3643  81 EHPRMGATDVIPFVPIRNVTMEECVELARELGKRIGEELGIPVYLYEEAATRPERK 136
 
Name Accession Description Interval E-value
FtcD TIGR02024
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
 1-136 1.93e-79

glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131079 [Multi-domain]  Cd Length: 298  Bit Score: 237.35  E-value: 1.93e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9887335      1 MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQG 80
Cdd:TIGR02024   1 MMKLVECVPNFSEGRNKEVIEKIVDAIIKTDNVKLLDVDMDPDHNRSVITFVGEPECVVNAALKLAKKAAELIDMRNHKG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 9887335     81 EHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPGLTAGLSCSLPVRR 136
Cdd:TIGR02024  81 EHPRMGAADVIPFIPVRNVTMEECVELAKEFGKRLGEELGVPVYLYEEAATRPERQ 136
FTCD_N pfam07837
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
 4-137 1.63e-76

Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.


Pssm-ID: 462283  Cd Length: 176  Bit Score: 225.43  E-value: 1.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9887335      4 LVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQGEHP 83
Cdd:pfam07837   1 LVECVPNFSEGRDKEVIEAIARAARSVPGVKLLDVFSDADHNRTVVTLVGEPEAVVEAALAAAKKAFELIDMRKHKGEHP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 9887335     84 RMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPGLTAGLSCSLPVRRG 137
Cdd:pfam07837  81 RMGAVDVIPFVPLRGVTMEECVELAKELAKRIGEELGVPVYLYEAAATRPERRN 134
GluFT COG3643
Glutamate formiminotransferase [Amino acid transport and metabolism];
1-136 2.23e-74

Glutamate formiminotransferase [Amino acid transport and metabolism];


Pssm-ID: 442860 [Multi-domain]  Cd Length: 303  Bit Score: 224.27  E-value: 2.23e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9887335    1 MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQG 80
Cdd:COG3643   1 MMKIVECVPNFSEGRDKEVIEAIVDAIRSVEGVKLLDYSPDADHNRTVVTFVGEPEAVKEAAFNAAKKAAELIDMTKHKG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 9887335   81 EHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPGLTAGLSCSLPVRR 136
Cdd:COG3643  81 EHPRMGATDVIPFVPIRNVTMEECVELARELGKRIGEELGIPVYLYEEAATRPERK 136
 
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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