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Conserved domains on  [gi|516951502|ref|WP_018181192|]
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glutamine amidotransferase [Kaistia granuli]

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 ...
5-255 5.85e-134

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: 377.58  E-value: 5.85e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502    5 KVLLVGESWMSSATHYKGFDQFGSVTFHLGAEPLVKALKDSEFELTYMQAHQVPTELPLTLEGLDAYDAIILSDIGSNSI 84
Cdd:pfam07090   1 KILLVGESWVSS*THIKGFDQFGSVTYHEGAKPLLEALEGSNYEVDYMPAHDAQERFPFTLEGLAAYDAIILSDIGSNTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502   85 LLHPDVWLQGKPMPNRVKLLREWTRKGGGLVMIGGYLTFQGIDGRGRWARTAVEDALPVTCLPHDDRIEVPEGFRAEVVg 164
Cdd:pfam07090  81 LLPPATWYRSQIVPNRLKLIKEYVAEGGGLLMIGGYLSFQGIDGKARFRNTPVEDVLPVTCLPWDDRVEIPEGCKAEIT- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502  165 DRAHPLLAGLDGEWPILLGANEVRLRDrpDVELLARLPDSegGHPLLVAGEFGEGRSVAWTSDIGPHWLPNSFVEWPGYA 244
Cdd:pfam07090 160 APEHPVVQGLSGEWPPLLGYNEVEARD--NAEVLATIPGD--QHPLLV*GEYGKGRTAAWTSDCSPHWLSPEFCDWEGYA 235
                         250
                  ....*....|.
gi 516951502  245 RLWKNVLGWVT 255
Cdd:pfam07090 236 RLWKNVLDWLT 246
 
Name Accession Description Interval E-value
GATase1_like pfam07090
Putative glutamine amidotransferase; This family consists of several hypothetical bacterial ...
5-255 5.85e-134

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: 377.58  E-value: 5.85e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502    5 KVLLVGESWMSSATHYKGFDQFGSVTFHLGAEPLVKALKDSEFELTYMQAHQVPTELPLTLEGLDAYDAIILSDIGSNSI 84
Cdd:pfam07090   1 KILLVGESWVSS*THIKGFDQFGSVTYHEGAKPLLEALEGSNYEVDYMPAHDAQERFPFTLEGLAAYDAIILSDIGSNTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502   85 LLHPDVWLQGKPMPNRVKLLREWTRKGGGLVMIGGYLTFQGIDGRGRWARTAVEDALPVTCLPHDDRIEVPEGFRAEVVg 164
Cdd:pfam07090  81 LLPPATWYRSQIVPNRLKLIKEYVAEGGGLLMIGGYLSFQGIDGKARFRNTPVEDVLPVTCLPWDDRVEIPEGCKAEIT- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502  165 DRAHPLLAGLDGEWPILLGANEVRLRDrpDVELLARLPDSegGHPLLVAGEFGEGRSVAWTSDIGPHWLPNSFVEWPGYA 244
Cdd:pfam07090 160 APEHPVVQGLSGEWPPLLGYNEVEARD--NAEVLATIPGD--QHPLLV*GEYGKGRTAAWTSDCSPHWLSPEFCDWEGYA 235
                         250
                  ....*....|.
gi 516951502  245 RLWKNVLGWVT 255
Cdd:pfam07090 236 RLWKNVLDWLT 246
COG5426 COG5426
Uncharacterized protein STM3548, contains class I glutamine amidotransferase domain [General ...
35-256 2.34e-56

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


Pssm-ID: 444178 [Multi-domain]  Cd Length: 738  Bit Score: 191.81  E-value: 2.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502  35 AEPLVKALKDSEFELTYMQAHQVPTELPLTLEGLDAYDAIILSDIGSNSILlhpdvwlqgkpmPNRVKLLREWTRKGGGL 114
Cdd:COG5426  348 LRFLRNALERPGIEVDHIPAHEALIGFPSTEEELFAYDVVILSDIGANTLL------------PNQLELLADYVERGGGL 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502 115 VMIGGYLTFqgidGRGRWARTAVEDALPVTCLPHddRIEVPEG-FRAEVVGD-RAHPLLAGLDG---------EWPILLG 183
Cdd:COG5426  416 LMAGGPLSF----GPGSYARTPLADVLPVELLPG--RGEVPEGpFRPELTEEgRRHPVTRGLPGsaanppawgELPPLLG 489
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516951502 184 ANEVrlRDRPDVELLARLPDsegGHPLLVAGEFGEGRSVAWTSDIGPHWLPNSFvEWPGYARLWKNVLGWVTK 256
Cdd:COG5426  490 YNRV--GAKPGAEVLATGPD---GDPLLVVGRYGKGRVAALASDQAWLWARGFF-GGGPYARLWRQLLRWLMK 556
A4_beta-galactosidase_middle_domain cd03143
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; ...
6-160 6.26e-05

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: 42.02  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502   6 VLLVGESWMSSATHYkgfdQFGSVTFHLGAEPLVKALKDSEFELTYMQAHQvptelpltleGLDAYDAIILSDIGSNSil 85
Cdd:cd03143    3 IVFDYESWWALELQP----QSAGLRYLDLALALYRALRELGIPVDVVPPDA----------DLSGYKLVVLPDLYLLS-- 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516951502  86 lhpdvwlqgkpmPNRVKLLREWTRKGGglVMIGGYLTFQGIDGRGRWARTAVedALPVTCLPHDDRIEVPEGFRA 160
Cdd:cd03143   67 ------------DATAAALRAYVENGG--TLVAGPRSGAVDEHDAIPLGLPP--PLGRLLGGLGVRVEELNAYGK 125
 
Name Accession Description Interval E-value
GATase1_like pfam07090
Putative glutamine amidotransferase; This family consists of several hypothetical bacterial ...
5-255 5.85e-134

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: 377.58  E-value: 5.85e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502    5 KVLLVGESWMSSATHYKGFDQFGSVTFHLGAEPLVKALKDSEFELTYMQAHQVPTELPLTLEGLDAYDAIILSDIGSNSI 84
Cdd:pfam07090   1 KILLVGESWVSS*THIKGFDQFGSVTYHEGAKPLLEALEGSNYEVDYMPAHDAQERFPFTLEGLAAYDAIILSDIGSNTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502   85 LLHPDVWLQGKPMPNRVKLLREWTRKGGGLVMIGGYLTFQGIDGRGRWARTAVEDALPVTCLPHDDRIEVPEGFRAEVVg 164
Cdd:pfam07090  81 LLPPATWYRSQIVPNRLKLIKEYVAEGGGLLMIGGYLSFQGIDGKARFRNTPVEDVLPVTCLPWDDRVEIPEGCKAEIT- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502  165 DRAHPLLAGLDGEWPILLGANEVRLRDrpDVELLARLPDSegGHPLLVAGEFGEGRSVAWTSDIGPHWLPNSFVEWPGYA 244
Cdd:pfam07090 160 APEHPVVQGLSGEWPPLLGYNEVEARD--NAEVLATIPGD--QHPLLV*GEYGKGRTAAWTSDCSPHWLSPEFCDWEGYA 235
                         250
                  ....*....|.
gi 516951502  245 RLWKNVLGWVT 255
Cdd:pfam07090 236 RLWKNVLDWLT 246
COG5426 COG5426
Uncharacterized protein STM3548, contains class I glutamine amidotransferase domain [General ...
35-256 2.34e-56

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


Pssm-ID: 444178 [Multi-domain]  Cd Length: 738  Bit Score: 191.81  E-value: 2.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502  35 AEPLVKALKDSEFELTYMQAHQVPTELPLTLEGLDAYDAIILSDIGSNSILlhpdvwlqgkpmPNRVKLLREWTRKGGGL 114
Cdd:COG5426  348 LRFLRNALERPGIEVDHIPAHEALIGFPSTEEELFAYDVVILSDIGANTLL------------PNQLELLADYVERGGGL 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502 115 VMIGGYLTFqgidGRGRWARTAVEDALPVTCLPHddRIEVPEG-FRAEVVGD-RAHPLLAGLDG---------EWPILLG 183
Cdd:COG5426  416 LMAGGPLSF----GPGSYARTPLADVLPVELLPG--RGEVPEGpFRPELTEEgRRHPVTRGLPGsaanppawgELPPLLG 489
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516951502 184 ANEVrlRDRPDVELLARLPDsegGHPLLVAGEFGEGRSVAWTSDIGPHWLPNSFvEWPGYARLWKNVLGWVTK 256
Cdd:COG5426  490 YNRV--GAKPGAEVLATGPD---GDPLLVVGRYGKGRVAALASDQAWLWARGFF-GGGPYARLWRQLLRWLMK 556
A4_beta-galactosidase_middle_domain cd03143
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; ...
6-160 6.26e-05

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: 42.02  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502   6 VLLVGESWMSSATHYkgfdQFGSVTFHLGAEPLVKALKDSEFELTYMQAHQvptelpltleGLDAYDAIILSDIGSNSil 85
Cdd:cd03143    3 IVFDYESWWALELQP----QSAGLRYLDLALALYRALRELGIPVDVVPPDA----------DLSGYKLVVLPDLYLLS-- 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516951502  86 lhpdvwlqgkpmPNRVKLLREWTRKGGglVMIGGYLTFQGIDGRGRWARTAVedALPVTCLPHDDRIEVPEGFRA 160
Cdd:cd03143   67 ------------DATAAALRAYVENGG--TLVAGPRSGAVDEHDAIPLGLPP--PLGRLLGGLGVRVEELNAYGK 125
ThuA pfam06283
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ...
34-222 7.19e-04

Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA appears to be involved in utilization of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium. ThuA is involved in the conversion of of disaccharides to their respective 3-keto derivatives.


Pssm-ID: 461867 [Multi-domain]  Cd Length: 213  Bit Score: 39.54  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502   34 GAEPLVKALKDSEFELTYmqahqvpTELP--LTLEGLDAYDAIilsdigsnsillhpdVWLQGKPM---PNRVKLLREWT 108
Cdd:pfam06283  19 GIEAIRKLGAENGFEVDA-------TEDAavFTDENLAQYDVV---------------VFLNTTGDvldEEQEAAFQRYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516951502  109 RKGGGLVMI-GGYLTFQG-------IDGRGRWARTAVEDAlpvtclphddrievpegfrAEVVGDRAHPLLAGLDGEWPI 180
Cdd:pfam06283  77 QAGGGFVGLhSAADTEYDwpwygklVGARFVAHDPAPQQA-------------------TVDVEDRSHPITAGLPAEWER 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 516951502  181 llgANEV--RLRDRPDVELLARLPDS--EGG------HPLLVAGEFGEGRSV 222
Cdd:pfam06283 138 ---TDEWynFKPNPPGNHVLATTDESsyDGGgnmgvdHPVAWTREDGAGRVF 186
 
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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