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Conserved domains on  [gi|567941419|ref|WP_024041877|]
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glutamine amidotransferase [Escherichia coli]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GATase1_like super family cl47177
Putative glutamine amidotransferase; This family consists of several hypothetical bacterial ...
9-247 3.47e-133

Putative glutamine amidotransferase; This family consists of several hypothetical bacterial proteins of around 250 residues in length. The function of this family is unknown. The structure of this cytoplasmic domain was solved by the Midwest Center for Structural Genomics (MCSG). The structure has been classified as part of the Class-I Glutamine amidotransferase superfamily owing to similarity with other known structures. The monomer combines with itself to form a hexamer, and this hexamer exposes a potential catalytic surface rich in Glu, Asp, Tyr, Ser.Trp and His residues.


The actual alignment was detected with superfamily member pfam07090:

Pssm-ID: 399821  Cd Length: 246  Bit Score: 375.66  E-value: 3.47e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419    9 KVLFIGESWHIHMIHSKGYDSFTSSKYEEGATWLLQCLKNSQVDVTYMPAHTVQIAFPEDVAQLEQYDAIVISDIGSNTF 88
Cdd:pfam07090   1 KILLVGESWVSS*THIKGFDQFGSVTYHEGAKPLLEALEGSNYEVDYMPAHDAQERFPFTLEGLAAYDAIILSDIGSNTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419   89 LLQNDTFYQLRIKPNALELIKEYVNNGGGLLMIGGYLSFMGIEAKANYKNTVLADVLPVTMLDGDDRVEKPEGVIAQPSQ 168
Cdd:pfam07090  81 LLPPATWYRSQIVPNRLKLIKEYVAEGGGLLMIGGYLSFQGIDGKARFRNTPVEDVLPVTCLPWDDRVEIPEGCKAEITA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419  169 PDHPVIKGFS-EYPFFLGYNRAIAKENAEVVLTINND--PLLVFGNYHNGKIACFMSDCSPHWGTQQFMSWSFYTALWVN 245
Cdd:pfam07090 161 PEHPVVQGLSgEWPPLLGYNEVEARDNAEVLATIPGDqhPLLV*GEYGKGRTAAWTSDCSPHWLSPEFCDWEGYARLWKN 240

                  ..
gi 567941419  246 IL 247
Cdd:pfam07090 241 VL 242
 
Name Accession Description Interval E-value
GATase1_like pfam07090
Putative glutamine amidotransferase; This family consists of several hypothetical bacterial ...
9-247 3.47e-133

Putative glutamine amidotransferase; This family consists of several hypothetical bacterial proteins of around 250 residues in length. The function of this family is unknown. The structure of this cytoplasmic domain was solved by the Midwest Center for Structural Genomics (MCSG). The structure has been classified as part of the Class-I Glutamine amidotransferase superfamily owing to similarity with other known structures. The monomer combines with itself to form a hexamer, and this hexamer exposes a potential catalytic surface rich in Glu, Asp, Tyr, Ser.Trp and His residues.


Pssm-ID: 399821  Cd Length: 246  Bit Score: 375.66  E-value: 3.47e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419    9 KVLFIGESWHIHMIHSKGYDSFTSSKYEEGATWLLQCLKNSQVDVTYMPAHTVQIAFPEDVAQLEQYDAIVISDIGSNTF 88
Cdd:pfam07090   1 KILLVGESWVSS*THIKGFDQFGSVTYHEGAKPLLEALEGSNYEVDYMPAHDAQERFPFTLEGLAAYDAIILSDIGSNTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419   89 LLQNDTFYQLRIKPNALELIKEYVNNGGGLLMIGGYLSFMGIEAKANYKNTVLADVLPVTMLDGDDRVEKPEGVIAQPSQ 168
Cdd:pfam07090  81 LLPPATWYRSQIVPNRLKLIKEYVAEGGGLLMIGGYLSFQGIDGKARFRNTPVEDVLPVTCLPWDDRVEIPEGCKAEITA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419  169 PDHPVIKGFS-EYPFFLGYNRAIAKENAEVVLTINND--PLLVFGNYHNGKIACFMSDCSPHWGTQQFMSWSFYTALWVN 245
Cdd:pfam07090 161 PEHPVVQGLSgEWPPLLGYNEVEARDNAEVLATIPGDqhPLLV*GEYGKGRTAAWTSDCSPHWLSPEFCDWEGYARLWKN 240

                  ..
gi 567941419  246 IL 247
Cdd:pfam07090 241 VL 242
COG5426 COG5426
Uncharacterized protein STM3548, contains class I glutamine amidotransferase domain [General ...
39-247 2.55e-66

Uncharacterized protein STM3548, contains class I glutamine amidotransferase domain [General function prediction only];


Pssm-ID: 444178 [Multi-domain]  Cd Length: 738  Bit Score: 218.39  E-value: 2.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419  39 ATWLLQCLKNSQVDVTYMPAHTVQIAFPEDVAQLEQYDAIVISDIGSNTFLlqndtfyqlrikPNALELIKEYVNNGGGL 118
Cdd:COG5426  348 LRFLRNALERPGIEVDHIPAHEALIGFPSTEEELFAYDVVILSDIGANTLL------------PNQLELLADYVERGGGL 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419 119 LMIGGYLSFmgieAKANYKNTVLADVLPVTMLDGddRVEKPEGVIA---QPSQPDHPVIKGF----------SEYPFFLG 185
Cdd:COG5426  416 LMAGGPLSF----GPGSYARTPLADVLPVELLPG--RGEVPEGPFRpelTEEGRRHPVTRGLpgsaanppawGELPPLLG 489
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567941419 186 YNRAIAKENAEVVLTI-NNDPLLVFGNYHNGKIACFMSDCSPHWGTQQFmSWSFYTALWVNIL 247
Cdd:COG5426  490 YNRVGAKPGAEVLATGpDGDPLLVVGRYGKGRVAALASDQAWLWARGFF-GGGPYARLWRQLL 551
A4_beta-galactosidase_middle_domain cd03143
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; ...
10-157 1.03e-15

A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.


Pssm-ID: 153237 [Multi-domain]  Cd Length: 154  Bit Score: 72.06  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419  10 VLFIGESWHIHMIHSKgydsFTSSKYEEGATWLLQCLKNSQVDVTYMPAHtvqiafpedvAQLEQYDAIVISDIGsntfl 89
Cdd:cd03143    3 IVFDYESWWALELQPQ----SAGLRYLDLALALYRALRELGIPVDVVPPD----------ADLSGYKLVVLPDLY----- 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567941419  90 lqndtfyqlRIKPNALELIKEYVNNGGglLMIGGYLSFMGIEAKANYKNTVLadVLPVTMLDGDDRVE 157
Cdd:cd03143   64 ---------LLSDATAAALRAYVENGG--TLVAGPRSGAVDEHDAIPLGLPP--PLGRLLGGLGVRVE 118
 
Name Accession Description Interval E-value
GATase1_like pfam07090
Putative glutamine amidotransferase; This family consists of several hypothetical bacterial ...
9-247 3.47e-133

Putative glutamine amidotransferase; This family consists of several hypothetical bacterial proteins of around 250 residues in length. The function of this family is unknown. The structure of this cytoplasmic domain was solved by the Midwest Center for Structural Genomics (MCSG). The structure has been classified as part of the Class-I Glutamine amidotransferase superfamily owing to similarity with other known structures. The monomer combines with itself to form a hexamer, and this hexamer exposes a potential catalytic surface rich in Glu, Asp, Tyr, Ser.Trp and His residues.


Pssm-ID: 399821  Cd Length: 246  Bit Score: 375.66  E-value: 3.47e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419    9 KVLFIGESWHIHMIHSKGYDSFTSSKYEEGATWLLQCLKNSQVDVTYMPAHTVQIAFPEDVAQLEQYDAIVISDIGSNTF 88
Cdd:pfam07090   1 KILLVGESWVSS*THIKGFDQFGSVTYHEGAKPLLEALEGSNYEVDYMPAHDAQERFPFTLEGLAAYDAIILSDIGSNTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419   89 LLQNDTFYQLRIKPNALELIKEYVNNGGGLLMIGGYLSFMGIEAKANYKNTVLADVLPVTMLDGDDRVEKPEGVIAQPSQ 168
Cdd:pfam07090  81 LLPPATWYRSQIVPNRLKLIKEYVAEGGGLLMIGGYLSFQGIDGKARFRNTPVEDVLPVTCLPWDDRVEIPEGCKAEITA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419  169 PDHPVIKGFS-EYPFFLGYNRAIAKENAEVVLTINND--PLLVFGNYHNGKIACFMSDCSPHWGTQQFMSWSFYTALWVN 245
Cdd:pfam07090 161 PEHPVVQGLSgEWPPLLGYNEVEARDNAEVLATIPGDqhPLLV*GEYGKGRTAAWTSDCSPHWLSPEFCDWEGYARLWKN 240

                  ..
gi 567941419  246 IL 247
Cdd:pfam07090 241 VL 242
COG5426 COG5426
Uncharacterized protein STM3548, contains class I glutamine amidotransferase domain [General ...
39-247 2.55e-66

Uncharacterized protein STM3548, contains class I glutamine amidotransferase domain [General function prediction only];


Pssm-ID: 444178 [Multi-domain]  Cd Length: 738  Bit Score: 218.39  E-value: 2.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419  39 ATWLLQCLKNSQVDVTYMPAHTVQIAFPEDVAQLEQYDAIVISDIGSNTFLlqndtfyqlrikPNALELIKEYVNNGGGL 118
Cdd:COG5426  348 LRFLRNALERPGIEVDHIPAHEALIGFPSTEEELFAYDVVILSDIGANTLL------------PNQLELLADYVERGGGL 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419 119 LMIGGYLSFmgieAKANYKNTVLADVLPVTMLDGddRVEKPEGVIA---QPSQPDHPVIKGF----------SEYPFFLG 185
Cdd:COG5426  416 LMAGGPLSF----GPGSYARTPLADVLPVELLPG--RGEVPEGPFRpelTEEGRRHPVTRGLpgsaanppawGELPPLLG 489
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567941419 186 YNRAIAKENAEVVLTI-NNDPLLVFGNYHNGKIACFMSDCSPHWGTQQFmSWSFYTALWVNIL 247
Cdd:COG5426  490 YNRVGAKPGAEVLATGpDGDPLLVVGRYGKGRVAALASDQAWLWARGFF-GGGPYARLWRQLL 551
A4_beta-galactosidase_middle_domain cd03143
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; ...
10-157 1.03e-15

A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.


Pssm-ID: 153237 [Multi-domain]  Cd Length: 154  Bit Score: 72.06  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567941419  10 VLFIGESWHIHMIHSKgydsFTSSKYEEGATWLLQCLKNSQVDVTYMPAHtvqiafpedvAQLEQYDAIVISDIGsntfl 89
Cdd:cd03143    3 IVFDYESWWALELQPQ----SAGLRYLDLALALYRALRELGIPVDVVPPD----------ADLSGYKLVVLPDLY----- 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567941419  90 lqndtfyqlRIKPNALELIKEYVNNGGglLMIGGYLSFMGIEAKANYKNTVLadVLPVTMLDGDDRVE 157
Cdd:cd03143   64 ---------LLSDATAAALRAYVENGG--TLVAGPRSGAVDEHDAIPLGLPP--PLGRLLGGLGVRVE 118
 
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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