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Conserved domains on  [gi|1834195055|gb|QJD13731|]
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Glutamate synthase large subunit, partial [Burkholderia cenocepacia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GltB3 super family cl41817
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ...
 1-193 6.98e-109

Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 is part of the Pathway/BioSystem: Glutamine biosynthesis


The actual alignment was detected with superfamily member COG0070:

Pssm-ID: 439840 [Multi-domain]  Cd Length: 1508  Bit Score: 340.34  E-value: 6.98e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055    1 CHLNTCPVGVATQDPVLRAKFKGQPEHVVNYFFFVAEEVREIMAQLGVAKFDDLIGRADLLDTRKGIEHWKAKGLDFSRV 80
Cdd:COG0070   1133 CHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPL 1212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055   81 FYQPEECEDVAPRHVDVQDHGLERALDHVLIEKAKAAIENGEHVSFIQPVRNVNRTVGAMLSGVIAKKHGHDGLADDAVH 160
Cdd:COG0070   1213 LYKPDVPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTIT 1292

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1834195055  161 IQLKGTAGQSFGAFLAKGVTLDLVGDGNDYVGK 193
Cdd:COG0070   1293 LRFTGSAGQSFGAFLAKGLTLELEGDANDYVGK 1325
 
Name Accession Description Interval E-value
GltB3 COG0070
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ...
 1-193 6.98e-109

Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439840 [Multi-domain]  Cd Length: 1508  Bit Score: 340.34  E-value: 6.98e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055    1 CHLNTCPVGVATQDPVLRAKFKGQPEHVVNYFFFVAEEVREIMAQLGVAKFDDLIGRADLLDTRKGIEHWKAKGLDFSRV 80
Cdd:COG0070   1133 CHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPL 1212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055   81 FYQPEECEDVAPRHVDVQDHGLERALDHVLIEKAKAAIENGEHVSFIQPVRNVNRTVGAMLSGVIAKKHGHDGLADDAVH 160
Cdd:COG0070   1213 LYKPDVPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTIT 1292

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1834195055  161 IQLKGTAGQSFGAFLAKGVTLDLVGDGNDYVGK 193
Cdd:COG0070   1293 LRFTGSAGQSFGAFLAKGLTLELEGDANDYVGK 1325
gltB PRK11750
glutamate synthase subunit alpha; Provisional
 1-193 9.60e-69

glutamate synthase subunit alpha; Provisional


Pssm-ID: 236968 [Multi-domain]  Cd Length: 1485  Bit Score: 226.68  E-value: 9.60e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055    1 CHLNTCPVGVATQDPVLRAK-FKGQPEHVVNYFFFVAEEVREIMAQLGVAKFDDLIGRADLLDTRKGIEHwKAKGLDFSR 79
Cdd:PRK11750  1111 CHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETA-KQQKLDLSP 1189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055   80 VFYQPEECEDvAPRHVDVQ-----DHGLeraLDHVLIEKAKAAIENGEHVSFIQPVRNVNRTVGAMLSGVIAKKHGHDGL 154
Cdd:PRK11750  1190 LLETAEPPAG-KALYCTEErnppfDKGL---LNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGM 1265

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1834195055  155 ADDAVHIQLKGTAGQSFGAFLAKGVTLDLVGDGNDYVGK 193
Cdd:PRK11750  1266 ADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGK 1304
gltB_C cd00982
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ...
 106-193 1.19e-43

gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS). GltS encodes a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites appear to occur in other domains within the protein, and not the domain in this CD. This particular domain has no known function, but it likely has a structural role as it interacts with the amidotransferase and FMN-binding domains of gltS.


Pssm-ID: 238482 [Multi-domain]  Cd Length: 251  Bit Score: 145.75  E-value: 1.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055 106 LDHVLIEKAK-AAIENGEHVSFIQPVRNVNRTVGAMLSGVIAKKHGHDGLADDAVHIQLKGTAGQSFGAFLAKGVTLDLV 184
Cdd:cd00982     1 LDDKLIADAEpALIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80


                  ....*....
gi 1834195055 185 GDGNDYVGK 193
Cdd:cd00982    81 GDANDYVGK 89
GXGXG pfam01493
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ...
 129-193 2.63e-35

GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran dehydrogenase subunit c (FwdC) and molybdenum formylmethanofuran dehydrogenase subunit c (FmdC). A repeated G-XX-G-XXX-G motif is seen in the alignment.


Pssm-ID: 460231 [Multi-domain]  Cd Length: 190  Bit Score: 122.52  E-value: 2.63e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834195055 129 PVRNVNRTVGAMLSGVIAKKHGHDGLADDAVHIQLKGTAGQSFGAFLAKGVTLDLVGDGNDYVGK 193
Cdd:pfam01493   2 EIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGK 66
 
Name Accession Description Interval E-value
GltB3 COG0070
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ...
 1-193 6.98e-109

Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439840 [Multi-domain]  Cd Length: 1508  Bit Score: 340.34  E-value: 6.98e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055    1 CHLNTCPVGVATQDPVLRAKFKGQPEHVVNYFFFVAEEVREIMAQLGVAKFDDLIGRADLLDTRKGIEHWKAKGLDFSRV 80
Cdd:COG0070   1133 CHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPL 1212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055   81 FYQPEECEDVAPRHVDVQDHGLERALDHVLIEKAKAAIENGEHVSFIQPVRNVNRTVGAMLSGVIAKKHGHDGLADDAVH 160
Cdd:COG0070   1213 LYKPDVPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTIT 1292

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1834195055  161 IQLKGTAGQSFGAFLAKGVTLDLVGDGNDYVGK 193
Cdd:COG0070   1293 LRFTGSAGQSFGAFLAKGLTLELEGDANDYVGK 1325
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
 1-193 9.27e-76

Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439839  Cd Length: 728  Bit Score: 240.92  E-value: 9.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055   1 CHLNTCPVGVATQDPVLRAKFK--GQPEHVVNYFFFVAEEVREIMAQLGVAKFDDLIGRADLLDTRKGiEHWKAKGLDFS 78
Cdd:COG0069   484 CHLNTCPVGVATQDPELRKGFVveGKPERVVNYFRFTAEEVREILAALGVRSPDELIGRHDLLRVRDG-EHWKAKGLDLS 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055  79 RVFYQPEECEDVAPRHVDVQDHGLERALDHVLIEKAKAAIENGEHVSFIQPVRNVNRTVGAMLSGVIAKKHGHDGLADDA 158
Cdd:COG0069   563 PLLYKPELPEGVPRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPVVLITNIRNNNRRVGGMLSGEIAKRYGGAGLPDDT 642

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1834195055 159 VHIQLKGTAGQSFGAFLAKGVTLDLVGDGNDYVGK 193
Cdd:COG0069   643 IILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGK 677
gltB PRK11750
glutamate synthase subunit alpha; Provisional
 1-193 9.60e-69

glutamate synthase subunit alpha; Provisional


Pssm-ID: 236968 [Multi-domain]  Cd Length: 1485  Bit Score: 226.68  E-value: 9.60e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055    1 CHLNTCPVGVATQDPVLRAK-FKGQPEHVVNYFFFVAEEVREIMAQLGVAKFDDLIGRADLLDTRKGIEHwKAKGLDFSR 79
Cdd:PRK11750  1111 CHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETA-KQQKLDLSP 1189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055   80 VFYQPEECEDvAPRHVDVQ-----DHGLeraLDHVLIEKAKAAIENGEHVSFIQPVRNVNRTVGAMLSGVIAKKHGHDGL 154
Cdd:PRK11750  1190 LLETAEPPAG-KALYCTEErnppfDKGL---LNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGM 1265

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1834195055  155 ADDAVHIQLKGTAGQSFGAFLAKGVTLDLVGDGNDYVGK 193
Cdd:PRK11750  1266 ADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGK 1304
gltB_C cd00982
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ...
 106-193 1.19e-43

gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS). GltS encodes a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites appear to occur in other domains within the protein, and not the domain in this CD. This particular domain has no known function, but it likely has a structural role as it interacts with the amidotransferase and FMN-binding domains of gltS.


Pssm-ID: 238482 [Multi-domain]  Cd Length: 251  Bit Score: 145.75  E-value: 1.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195055 106 LDHVLIEKAK-AAIENGEHVSFIQPVRNVNRTVGAMLSGVIAKKHGHDGLADDAVHIQLKGTAGQSFGAFLAKGVTLDLV 184
Cdd:cd00982     1 LDDKLIADAEpALIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80


                  ....*....
gi 1834195055 185 GDGNDYVGK 193
Cdd:cd00982    81 GDANDYVGK 89
GXGXG pfam01493
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ...
 129-193 2.63e-35

GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran dehydrogenase subunit c (FwdC) and molybdenum formylmethanofuran dehydrogenase subunit c (FmdC). A repeated G-XX-G-XXX-G motif is seen in the alignment.


Pssm-ID: 460231 [Multi-domain]  Cd Length: 190  Bit Score: 122.52  E-value: 2.63e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834195055 129 PVRNVNRTVGAMLSGVIAKKHGHDGLADDAVHIQLKGTAGQSFGAFLAKGVTLDLVGDGNDYVGK 193
Cdd:pfam01493   2 EIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGK 66
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 1-48 2.17e-21

Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 396287 [Multi-domain]  Cd Length: 367  Bit Score: 89.70  E-value: 2.17e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1834195055   1 CHLNTCPVGVATQDPVLR--AKFKGQPEHVVNYFFFVAEEVREIMAQLGV 48
Cdd:pfam01645 317 CHTNTCPVGVATQDPELRkrLDFEGAPERVVNYFRFLAEEVRELLAALGI 366
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 1-61 2.84e-21

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202 [Multi-domain]  Cd Length: 392  Bit Score: 89.52  E-value: 2.84e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834195055   1 CHLNTCPVGVATQDPVL--RAKFKGQPEHVVNYFFFVAEEVREIMAQLGVAKfDDLIGRADLL 61
Cdd:cd02808   329 CHTNTCPVGVATQDPELrrRLDVEGKAERVANYLKSLAEELRELAAALGKRS-LELLGRSDLL 390
GXGXG cd00504
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ...
 135-193 1.35e-14

GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS), in subunit C of tungsten formylmethanofuran dehydrogenase (FwdC) and in subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC). It is also found in a primarily archeal group of proteins predicted to encode part of the large subunit of GltS. It is characterized by a repeated GXXGXXXG motif. GltS is a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites occur in other domains within the protein or or encoded by separate genes, and are not present in the domain in this CD. FwdC and FmdC are reversible ion pumps that catalyze the formylation and deformylation of methanofuran in hyperthermophiles and bacteria. They require the presence of either tungstun (FwdC) or molybdenum (FmdC). The specific function of this domain also remains unidentified in the formylmethanofuran dehydrogenases.


Pssm-ID: 238281 [Multi-domain]  Cd Length: 149  Bit Score: 67.59  E-value: 1.35e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1834195055 135 RTVGAMLSGVIAKKhghDGLADDAVHIQLKGTAGQSFGAFLAkGVTLDLVGDGNDYVGK 193
Cdd:cd00504     1 RAVGTRGSRYIGKR---PGLPEDTVEIIINGSAGQSFGAFMA-GGTITVEGNANDYVGK 55
 
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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