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Conserved domains on  [gi|15600312|ref|NP_253806|]
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glutamine synthetase [Pseudomonas aeruginosa PAO1]

Protein Classification

glutamine synthetase family protein( domain architecture ID 1000788)

glutamine synthetase family protein such as glutamine synthetase that catalyzes the condensation of glutamate and ammonia to form glutamine

Gene Ontology:  GO:0004356|GO:0006542
SCOP:  4001002|4002006

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
glnA super family cl32375
glutamate--ammonia ligase;
7-469 0e+00

glutamate--ammonia ligase;


The actual alignment was detected with superfamily member PRK09469:

Pssm-ID: 181884 [Multi-domain]  Cd Length: 469  Bit Score: 867.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312    7 QLIKDHDVKWVDLRFTDTKGKQQHVTMPARDaLDDEFFEAGKMFDGSSIAGWKGIEASDMILMPDDSTAVLDPFTEEPTL 86
Cdd:PRK09469   8 TMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQ-VNADFFEEGKMFDGSSIGGWKGINESDMVLMPDASTAVLDPFFEDSTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   87 ILVCDIIEPSTMQGYERDPRNIAKRAEEYLKSTGIGDTVFVGPEPEFFIFDEVKFKSDISGSMFKIFSEQASWNTDADIE 166
Cdd:PRK09469  87 IIRCDILEPGTMQGYDRDPRSIAKRAEDYLRSTGIADTVLFGPEPEFFLFDDIRFGSSISGSHVAIDDIEAAWNSGTKYE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  167 SGNKGHRPGVKGGYFPVPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATAGQNEIGVKFNTLVAKADEVQTLKYCVHNV 246
Cdd:PRK09469 167 GGNKGHRPGVKGGYFPVPPVDSSQDIRSAMCLVMEEMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  247 ADAYGKTVTFMPKPLYGDNGSGMHVHMSISKDGKNTFAGEGYAGLSETALYFIGGIIKHGKALNGFTNPSTNSYKRLVPG 326
Cdd:PRK09469 247 AHAFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLFAGDKYAGLSEQALYYIGGIIKHAKAINALANPTTNSYKRLVPG 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  327 FEAPVMLAYSARNRSASIRIPYVSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAADKNLYDLPPEEAK 406
Cdd:PRK09469 327 YEAPVMLAYSARNRSASIRIPVVASPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNLYDLPPEEAA 406
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600312  407 EIPQVCGSLKEALEELDKGRAFLTKGGVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLYYSV 469
Cdd:PRK09469 407 EIPQVAGSLEEALNALDADREFLTAGGVFTDDAIDAYIALRREEVDRVRMTPHPVEFELYYSV 469
 
Name Accession Description Interval E-value
glnA PRK09469
glutamate--ammonia ligase;
7-469 0e+00

glutamate--ammonia ligase;


Pssm-ID: 181884 [Multi-domain]  Cd Length: 469  Bit Score: 867.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312    7 QLIKDHDVKWVDLRFTDTKGKQQHVTMPARDaLDDEFFEAGKMFDGSSIAGWKGIEASDMILMPDDSTAVLDPFTEEPTL 86
Cdd:PRK09469   8 TMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQ-VNADFFEEGKMFDGSSIGGWKGINESDMVLMPDASTAVLDPFFEDSTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   87 ILVCDIIEPSTMQGYERDPRNIAKRAEEYLKSTGIGDTVFVGPEPEFFIFDEVKFKSDISGSMFKIFSEQASWNTDADIE 166
Cdd:PRK09469  87 IIRCDILEPGTMQGYDRDPRSIAKRAEDYLRSTGIADTVLFGPEPEFFLFDDIRFGSSISGSHVAIDDIEAAWNSGTKYE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  167 SGNKGHRPGVKGGYFPVPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATAGQNEIGVKFNTLVAKADEVQTLKYCVHNV 246
Cdd:PRK09469 167 GGNKGHRPGVKGGYFPVPPVDSSQDIRSAMCLVMEEMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  247 ADAYGKTVTFMPKPLYGDNGSGMHVHMSISKDGKNTFAGEGYAGLSETALYFIGGIIKHGKALNGFTNPSTNSYKRLVPG 326
Cdd:PRK09469 247 AHAFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLFAGDKYAGLSEQALYYIGGIIKHAKAINALANPTTNSYKRLVPG 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  327 FEAPVMLAYSARNRSASIRIPYVSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAADKNLYDLPPEEAK 406
Cdd:PRK09469 327 YEAPVMLAYSARNRSASIRIPVVASPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNLYDLPPEEAA 406
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600312  407 EIPQVCGSLKEALEELDKGRAFLTKGGVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLYYSV 469
Cdd:PRK09469 407 EIPQVAGSLEEALNALDADREFLTAGGVFTDDAIDAYIALRREEVDRVRMTPHPVEFELYYSV 469
GlnA TIGR00653
glutamine synthetase, type I; Alternate name: glutamate--ammonia ligase. This model represents ...
7-468 0e+00

glutamine synthetase, type I; Alternate name: glutamate--ammonia ligase. This model represents the dodecameric form, which can be subdivided into 1-alpha and 1-beta forms. The phylogeny of the 1-alpha and 1-beta forms appears polyphyletic. E. coli, Synechocystis PCC6803, Aquifex aeolicus, and the crenarcheon Sulfolobus acidocaldarius have form 1-beta, while Bacillus subtilis, Thermotoga maritima, and various euryarchaea has form 1-alpha. The 1-beta dodecamer from the crenarcheon Sulfolobus acidocaldarius differs from that in E. coli in that it is not regulated by adenylylation. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273198 [Multi-domain]  Cd Length: 459  Bit Score: 712.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312     7 QLIKDHDVKWVDLRFTDTKGKQQHVTMPARdALDDEFFEAGKMFDGSSIAGWKGIEASDMILMPDDSTAVLDPFTEEPTL 86
Cdd:TIGR00653   5 KLIKEENVKFVDLRFTDIKGKPQHVEIPAS-ALDKEAFEEGIMFDGSSIRGFQGIEESDMLLKPDPSTAVIDPWRAEKTL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312    87 ILVCDIIEPSTMQGYERDPRNIAKRAEEYLKStGIGDTVFVGPEPEFFIFDEVKFKSDISGSMFKIFSEQASWNTdadiE 166
Cdd:TIGR00653  84 RVICDVYEPFTGEPYERDPRSIAKRAEEYLKS-GIGDTAYFGPEPEFFLFDSVEFGSLANGSFYEVDSEEGRWNE----E 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   167 SGNKGHRPGVKGGYFPVPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATaGQNEIGVKFNTLVAKADEVQTLKYCVHNV 246
Cdd:TIGR00653 159 SGNRGYKPRDKGGYFPVAPTDTAVDIRREMVLYLEQLGFDVEVHHHEVAT-GQHEIDFKFDTLLKTADDIQTYKYVVKNV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   247 ADAYGKTVTFMPKPLYGDNGSGMHVHMSISKDGKNTFAGEGYAGLSETALYFIGGIIKHGKALNGFTNPSTNSYKRLVPG 326
Cdd:TIGR00653 238 ARKHGKTATFMPKPLFGDNGSGMHCHQSLWKDGENLFAGEEYAGLSETALYYIGGILKHAKALAAFTNPTVNSYKRLVPG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   327 FEAPVMLAYSARNRSASIRIPYVSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAADKNLYDLPPEEAK 406
Cdd:TIGR00653 318 YEAPVYLAYSARNRSALIRIPASGNPKAKRIEFRFPDPSANPYLAFAAMLMAGLDGIKNKIDPGEPVDKNLYELSPEELR 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600312   407 E--IPQVCGSLKEALEELDKGRafLTKGGVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLYYS 468
Cdd:TIGR00653 398 EkgIPQLPGSLEEALDELESDH--LVEGGVFGEEFIEAFIELKRKEWDPYRLRPHPWEFELYYD 459
GlnA COG0174
Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of ...
1-468 0e+00

Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439944 [Multi-domain]  Cd Length: 440  Bit Score: 653.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   1 MSYKS----HQLIKDHDVKWVDLRFTDTKGKQQHVTMPARDAldDEFFEAGKMFDGSSIAGWKGIEASDMILMPDDSTAV 76
Cdd:COG0174   1 MSKLTveevLAFLKERGVKFVDLQFTDINGVLRGKRVPASEL--EKALEEGIGFDGSSIEGFVEIGESDMVLVPDPSTLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  77 LDPFTEEPTLILVCDIIEPsTMQGYERDPRNIAKRAEEYLKSTGIgdTVFVGPEPEFFIFDEvkfksdisgsmfkifseq 156
Cdd:COG0174  79 ILPWRPEPTARVICDVYDP-DGEPYEGDPRNVLKRVLARLAETGL--TPYVGPELEFFLFDD------------------ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312 157 aswntDADiESGNKGHRPGVKGGYFPVPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATaGQNEIGVKFNTLVAKADEV 236
Cdd:COG0174 138 -----DSD-EKGNRGLRPRDKGGYYDLAPLDRFEDFRREIVLALEAMGIPVETSHHEVAP-GQHEINLRYADALTAADRV 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312 237 QTLKYCVHNVADAYGKTVTFMPKPLYGDNGSGMHVHMSISK-DGKNTFAGE-GYAGLSETALYFIGGIIKHGKALNGFTN 314
Cdd:COG0174 211 VLFKYVVKEVARRHGLTATFMPKPFAGDNGSGMHVHQSLWDaDGKNLFADPdGYAGLSELARHFIGGLLKHAPALTAFTA 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312 315 PSTNSYKRLVPGFEAPVMLAYSARNRSASIRIPyVSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAAD 394
Cdd:COG0174 291 PTVNSYKRLVPGYEAPVNIAWGYDNRSAAIRIP-GGSPKATRIEYRVPDADANPYLAFAALLAAGLDGIENKLEPGEPVD 369
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600312 395 KNLYDLPPEEAKEIPQVCGSLKEALEELDKGrAFLTkgGVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLYYS 468
Cdd:COG0174 370 GNAYELSPEERAGIPRLPRSLEEALDALEAD-EFLR--EVLGEDFVDHYIALKRAEWEEFRRRVTPWERERYLE 440
Gln-synt_C pfam00120
Glutamine synthetase, catalytic domain;
103-466 0e+00

Glutamine synthetase, catalytic domain;


Pssm-ID: 425473 [Multi-domain]  Cd Length: 343  Bit Score: 540.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   103 RDPRNIAKRAEEYLKSTGIgdTVFVGPEPEFFIFDEVKFKsDISGSMFKIFSEQaswntdadiesgnkGHRPGVKGGYFP 182
Cdd:pfam00120   1 RDPRSILKRALARLASLGL--TAYVGPELEFFLFDRVEDG-NPNGPFYPPDSEG--------------GYRPADKGGYFD 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   183 VPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATaGQNEIGVKFNTLVAKADEVQTLKYCVHNVADAYGKTVTFMPKPLY 262
Cdd:pfam00120  64 VAPVDSAQDLRREIVDALEAMGIEVEASHHEVAP-GQHEIDFRFDDALKAADNAQTFKYVVKNVARKHGLTATFMPKPFF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   263 GDNGSGMHVHMSISKDGKNTFAGE-GYAGLSETALYFIGGIIKHGKALNGFTNPSTNSYKRLVPGFEAPVMLAYSARNRS 341
Cdd:pfam00120 143 GDNGSGMHVHQSLWKDGKNLFADPdGEYGLSETARHFIAGILKHAPALTALTNPTVNSYKRLVPGYEAPVYLAWGARNRS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   342 ASIRIPYvSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAADKNLYDLPPEEAKEIPQVCGSLKEALEE 421
Cdd:pfam00120 223 AALRIPA-GSPKARRVEVRSPDPDANPYLAFAALLAAGLDGIENKIDPGEPVDGNLYELTPEERKGIPTLPSSLEEALDA 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 15600312   422 LDKGrAFLTKggVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLY 466
Cdd:pfam00120 302 LEED-ELLKE--ALGEHFIEAYIAVKRAEWEEFRTAVHPWEFERY 343
 
Name Accession Description Interval E-value
glnA PRK09469
glutamate--ammonia ligase;
7-469 0e+00

glutamate--ammonia ligase;


Pssm-ID: 181884 [Multi-domain]  Cd Length: 469  Bit Score: 867.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312    7 QLIKDHDVKWVDLRFTDTKGKQQHVTMPARDaLDDEFFEAGKMFDGSSIAGWKGIEASDMILMPDDSTAVLDPFTEEPTL 86
Cdd:PRK09469   8 TMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQ-VNADFFEEGKMFDGSSIGGWKGINESDMVLMPDASTAVLDPFFEDSTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   87 ILVCDIIEPSTMQGYERDPRNIAKRAEEYLKSTGIGDTVFVGPEPEFFIFDEVKFKSDISGSMFKIFSEQASWNTDADIE 166
Cdd:PRK09469  87 IIRCDILEPGTMQGYDRDPRSIAKRAEDYLRSTGIADTVLFGPEPEFFLFDDIRFGSSISGSHVAIDDIEAAWNSGTKYE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  167 SGNKGHRPGVKGGYFPVPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATAGQNEIGVKFNTLVAKADEVQTLKYCVHNV 246
Cdd:PRK09469 167 GGNKGHRPGVKGGYFPVPPVDSSQDIRSAMCLVMEEMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  247 ADAYGKTVTFMPKPLYGDNGSGMHVHMSISKDGKNTFAGEGYAGLSETALYFIGGIIKHGKALNGFTNPSTNSYKRLVPG 326
Cdd:PRK09469 247 AHAFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLFAGDKYAGLSEQALYYIGGIIKHAKAINALANPTTNSYKRLVPG 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  327 FEAPVMLAYSARNRSASIRIPYVSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAADKNLYDLPPEEAK 406
Cdd:PRK09469 327 YEAPVMLAYSARNRSASIRIPVVASPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNLYDLPPEEAA 406
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600312  407 EIPQVCGSLKEALEELDKGRAFLTKGGVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLYYSV 469
Cdd:PRK09469 407 EIPQVAGSLEEALNALDADREFLTAGGVFTDDAIDAYIALRREEVDRVRMTPHPVEFELYYSV 469
GlnA TIGR00653
glutamine synthetase, type I; Alternate name: glutamate--ammonia ligase. This model represents ...
7-468 0e+00

glutamine synthetase, type I; Alternate name: glutamate--ammonia ligase. This model represents the dodecameric form, which can be subdivided into 1-alpha and 1-beta forms. The phylogeny of the 1-alpha and 1-beta forms appears polyphyletic. E. coli, Synechocystis PCC6803, Aquifex aeolicus, and the crenarcheon Sulfolobus acidocaldarius have form 1-beta, while Bacillus subtilis, Thermotoga maritima, and various euryarchaea has form 1-alpha. The 1-beta dodecamer from the crenarcheon Sulfolobus acidocaldarius differs from that in E. coli in that it is not regulated by adenylylation. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273198 [Multi-domain]  Cd Length: 459  Bit Score: 712.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312     7 QLIKDHDVKWVDLRFTDTKGKQQHVTMPARdALDDEFFEAGKMFDGSSIAGWKGIEASDMILMPDDSTAVLDPFTEEPTL 86
Cdd:TIGR00653   5 KLIKEENVKFVDLRFTDIKGKPQHVEIPAS-ALDKEAFEEGIMFDGSSIRGFQGIEESDMLLKPDPSTAVIDPWRAEKTL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312    87 ILVCDIIEPSTMQGYERDPRNIAKRAEEYLKStGIGDTVFVGPEPEFFIFDEVKFKSDISGSMFKIFSEQASWNTdadiE 166
Cdd:TIGR00653  84 RVICDVYEPFTGEPYERDPRSIAKRAEEYLKS-GIGDTAYFGPEPEFFLFDSVEFGSLANGSFYEVDSEEGRWNE----E 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   167 SGNKGHRPGVKGGYFPVPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATaGQNEIGVKFNTLVAKADEVQTLKYCVHNV 246
Cdd:TIGR00653 159 SGNRGYKPRDKGGYFPVAPTDTAVDIRREMVLYLEQLGFDVEVHHHEVAT-GQHEIDFKFDTLLKTADDIQTYKYVVKNV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   247 ADAYGKTVTFMPKPLYGDNGSGMHVHMSISKDGKNTFAGEGYAGLSETALYFIGGIIKHGKALNGFTNPSTNSYKRLVPG 326
Cdd:TIGR00653 238 ARKHGKTATFMPKPLFGDNGSGMHCHQSLWKDGENLFAGEEYAGLSETALYYIGGILKHAKALAAFTNPTVNSYKRLVPG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   327 FEAPVMLAYSARNRSASIRIPYVSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAADKNLYDLPPEEAK 406
Cdd:TIGR00653 318 YEAPVYLAYSARNRSALIRIPASGNPKAKRIEFRFPDPSANPYLAFAAMLMAGLDGIKNKIDPGEPVDKNLYELSPEELR 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600312   407 E--IPQVCGSLKEALEELDKGRafLTKGGVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLYYS 468
Cdd:TIGR00653 398 EkgIPQLPGSLEEALDELESDH--LVEGGVFGEEFIEAFIELKRKEWDPYRLRPHPWEFELYYD 459
GlnA COG0174
Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of ...
1-468 0e+00

Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439944 [Multi-domain]  Cd Length: 440  Bit Score: 653.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   1 MSYKS----HQLIKDHDVKWVDLRFTDTKGKQQHVTMPARDAldDEFFEAGKMFDGSSIAGWKGIEASDMILMPDDSTAV 76
Cdd:COG0174   1 MSKLTveevLAFLKERGVKFVDLQFTDINGVLRGKRVPASEL--EKALEEGIGFDGSSIEGFVEIGESDMVLVPDPSTLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  77 LDPFTEEPTLILVCDIIEPsTMQGYERDPRNIAKRAEEYLKSTGIgdTVFVGPEPEFFIFDEvkfksdisgsmfkifseq 156
Cdd:COG0174  79 ILPWRPEPTARVICDVYDP-DGEPYEGDPRNVLKRVLARLAETGL--TPYVGPELEFFLFDD------------------ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312 157 aswntDADiESGNKGHRPGVKGGYFPVPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATaGQNEIGVKFNTLVAKADEV 236
Cdd:COG0174 138 -----DSD-EKGNRGLRPRDKGGYYDLAPLDRFEDFRREIVLALEAMGIPVETSHHEVAP-GQHEINLRYADALTAADRV 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312 237 QTLKYCVHNVADAYGKTVTFMPKPLYGDNGSGMHVHMSISK-DGKNTFAGE-GYAGLSETALYFIGGIIKHGKALNGFTN 314
Cdd:COG0174 211 VLFKYVVKEVARRHGLTATFMPKPFAGDNGSGMHVHQSLWDaDGKNLFADPdGYAGLSELARHFIGGLLKHAPALTAFTA 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312 315 PSTNSYKRLVPGFEAPVMLAYSARNRSASIRIPyVSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAAD 394
Cdd:COG0174 291 PTVNSYKRLVPGYEAPVNIAWGYDNRSAAIRIP-GGSPKATRIEYRVPDADANPYLAFAALLAAGLDGIENKLEPGEPVD 369
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600312 395 KNLYDLPPEEAKEIPQVCGSLKEALEELDKGrAFLTkgGVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLYYS 468
Cdd:COG0174 370 GNAYELSPEERAGIPRLPRSLEEALDALEAD-EFLR--EVLGEDFVDHYIALKRAEWEEFRRRVTPWERERYLE 440
Gln-synt_C pfam00120
Glutamine synthetase, catalytic domain;
103-466 0e+00

Glutamine synthetase, catalytic domain;


Pssm-ID: 425473 [Multi-domain]  Cd Length: 343  Bit Score: 540.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   103 RDPRNIAKRAEEYLKSTGIgdTVFVGPEPEFFIFDEVKFKsDISGSMFKIFSEQaswntdadiesgnkGHRPGVKGGYFP 182
Cdd:pfam00120   1 RDPRSILKRALARLASLGL--TAYVGPELEFFLFDRVEDG-NPNGPFYPPDSEG--------------GYRPADKGGYFD 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   183 VPPVDHDHEIRTAMCNALEEMGLVVEVHHHEVATaGQNEIGVKFNTLVAKADEVQTLKYCVHNVADAYGKTVTFMPKPLY 262
Cdd:pfam00120  64 VAPVDSAQDLRREIVDALEAMGIEVEASHHEVAP-GQHEIDFRFDDALKAADNAQTFKYVVKNVARKHGLTATFMPKPFF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   263 GDNGSGMHVHMSISKDGKNTFAGE-GYAGLSETALYFIGGIIKHGKALNGFTNPSTNSYKRLVPGFEAPVMLAYSARNRS 341
Cdd:pfam00120 143 GDNGSGMHVHQSLWKDGKNLFADPdGEYGLSETARHFIAGILKHAPALTALTNPTVNSYKRLVPGYEAPVYLAWGARNRS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   342 ASIRIPYvSSPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAADKNLYDLPPEEAKEIPQVCGSLKEALEE 421
Cdd:pfam00120 223 AALRIPA-GSPKARRVEVRSPDPDANPYLAFAALLAAGLDGIENKIDPGEPVDGNLYELTPEERKGIPTLPSSLEEALDA 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 15600312   422 LDKGrAFLTKggVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLY 466
Cdd:pfam00120 302 LEED-ELLKE--ALGEHFIEAYIAVKRAEWEEFRTAVHPWEFERY 343
gln_synth_III TIGR03105
glutamine synthetase, type III; This family consists of the type III isozyme of glutamine ...
7-466 4.61e-83

glutamine synthetase, type III; This family consists of the type III isozyme of glutamine synthetase, originally described in Rhizobium meliloti, where types I and II also occur.


Pssm-ID: 274431 [Multi-domain]  Cd Length: 435  Bit Score: 262.69  E-value: 4.61e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312     7 QLIKDHDVKWVDLRFTDTKGKQQHVTMPArDALDDeFFEAGKMFDGSSIAGWkGIEA--SDMILMPDDSTAVLDPFTEEP 84
Cdd:TIGR03105   3 ALARDKGIKYFLASFVDLHGVQKAKLVPA-EAIDH-MATGGAGFAGFAAWGL-GQSPadPDLMAIPDLDSLTQLPWQPGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312    85 TLIlVCDiiepSTMQG--YERDPRNIAKRAEEYLKSTGIgdTVFVGPEPEFFIFDEvkfKSDISGSMFKIFSEQASWNTD 162
Cdd:TIGR03105  80 AWV-AAD----LHVNGkpYPQAPRVVLKRQLAEAAELGL--TLNTGVECEFFLLRR---DEDGSLSIADRADTLAKPCYD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   163 ADiesgnkghrpGVKGGYfpvppvdhdhEIRTAMCNALEEMGLVVEVHHHEVATaGQNEIGVKFNTLVAKADEVQTLKYC 242
Cdd:TIGR03105 150 QR----------GLMRRY----------DVLTEISDAMNALGWDPYQNDHEDAN-GQFEMNFTYADALTTADRHAFFRYM 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   243 VHNVADAYGKTVTFMPKPLYGDNGSGMHVHMSI-SKDGKNTFA---GEGYAGLSETALYFIGGIIKHGKALNGFTNPSTN 318
Cdd:TIGR03105 209 VKEIAEKHGMRATFMPKPFADLTGNGCHFHLSLwDEDGRNLFAddsDPNGLGLSKLAYHFIGGILHHAPALCAVLAPTVN 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   319 SYKRLV-----PGFE-APVMLAYSARNRSASIRIpyvssPKARRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDA 392
Cdd:TIGR03105 289 SYKRLNaprttSGATwAPNFISYGGNNRTHMVRI-----PDPGRFELRLADGAANPYLAQAAILAAGLDGIERKLDPGPP 363
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600312   393 ADKNLY--DLPPEEAKEIPQvcgSLKEALEELDKGRAFltkGGVFTDEFIDAYIELKSEEEIKVRTFVHPLEYDLY 466
Cdd:TIGR03105 364 RDINLYaeELAARGVETLPQ---NLLEALRALEADPLL---AEALGAEFVDEFLKLKRQEWEEYHRHVSDWEIDRY 433
Gln-synt_N pfam03951
Glutamine synthetase, beta-Grasp domain;
13-95 6.80e-41

Glutamine synthetase, beta-Grasp domain;


Pssm-ID: 427610 [Multi-domain]  Cd Length: 82  Bit Score: 140.73  E-value: 6.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312    13 DVKWVDLRFTDTKGKQQHVTMPArDALDDEFFEAGKMFDGSSIAGWKGIEASDMILMPDDSTAVLDPFTEEPTLILVCDI 92
Cdd:pfam03951   1 NVKFVDLRFTDILGKLKHVTIPA-SELDEDAFEEGIGFDGSSIEGFARIEESDMLLKPDPSTAFIDPFRPEPTARVICDV 79

                  ...
gi 15600312    93 IEP 95
Cdd:pfam03951  80 YDP 82
PLN02284 PLN02284
glutamine synthetase
16-370 5.87e-08

glutamine synthetase


Pssm-ID: 177922 [Multi-domain]  Cd Length: 354  Bit Score: 54.31  E-value: 5.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   16 WVDLRFTDTKGKQQHVTMPARDALDDEFFEagkmFDGSSIAGWKGiEASDMILMPddSTAVLDPFTEEPTLILVCDIIEP 95
Cdd:PLN02284  25 WIGGSGMDLRSKARTLPGPVTDPSKLPKWN----YDGSSTGQAPG-EDSEVILYP--QAIFKDPFRGGNNILVMCDAYTP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   96 STmqgyERDPRNIAKRAEEYLKSTGIGDTV-FVGPEPEFFIFDevkfksdisgsmfKIFSEQASWNtdadiesgnKGHRP 174
Cdd:PLN02284  98 AG----EPIPTNKRAKAAKIFSHPDVAAEEpWYGIEQEYTLLQ-------------KDVKWPLGWP---------VGGYP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  175 GVKGGYFPVPPVD--HDHEIRTAMCNALEEMGLVVEVHHHEVaTAGQNEIGVKFNTLVAKADEVQTLKYCVHNVADAYGK 252
Cdd:PLN02284 152 GPQGPYYCGVGADkaFGRDIVDAHYKACLYAGINISGINGEV-MPGQWEFQVGPVVGISAGDQLWVARYILERITEIAGV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  253 TVTFMPKPLYGD-NGSGMHVHMSiSKDGKNtfagEGYAGLSETALYFIGgiIKHGK--ALNGFTNPstnsyKRLVPGFEA 329
Cdd:PLN02284 231 VVSFDPKPIPGDwNGAGAHTNYS-TKSMRE----DGGYEVIKKAIEKLG--LRHKEhiAAYGEGNE-----RRLTGKHET 298
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 15600312  330 PVM--LAYSARNRSASIRIPyVSSPKARR--IEARFPDPAANPYL 370
Cdd:PLN02284 299 ADIntFSWGVANRGASIRVG-RDTEKEGKgyFEDRRPASNMDPYV 342
PLN03036 PLN03036
glutamine synthetase; Provisional
16-375 3.84e-07

glutamine synthetase; Provisional


Pssm-ID: 178603 [Multi-domain]  Cd Length: 432  Bit Score: 52.28  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   16 WVDLRFTDTKGKQQHVTMPARDAlddefFEAGKM-FDGSSIAGWKGiEASDMILMPDdstAVL-DPFTEEPTLILVCDII 93
Cdd:PLN03036  85 WIGGSGIDLRSKSRTISKPVEHP-----SELPKWnYDGSSTGQAPG-EDSEVILYPQ---AIFkDPFRGGNNILVICDTY 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312   94 EPSTmqgyERDPRNIAKRAEEYLKSTGIGDTVfvgpePEFFIFDEvkfksdisgsmFKIFSEQASWNTDADIesgnkGHR 173
Cdd:PLN03036 156 TPAG----EPIPTNKRHRAAEIFSNKKVVDEV-----PWFGIEQE-----------YTLLQQNVKWPLGWPV-----GAY 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  174 PGVKGGYFPVPPVDHD--HEIRTAMCNALEEMGLVVEVHHHEVaTAGQNEIGVKFNTLVAKADEVQTLKYCVHNVADAYG 251
Cdd:PLN03036 211 PGPQGPYYCGAGADKSfgRDISDAHYKACLYAGINISGTNGEV-MPGQWEYQVGPSVGIDAGDHIWCSRYILERITEQAG 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600312  252 KTVTFMPKPLYGD-NGSGMHVHMS---ISKDGkntfageGYAGLSETALYFiggIIKHGKALNGFtnpSTNSYKRLVPGF 327
Cdd:PLN03036 290 VVLTLDPKPIEGDwNGAGCHTNYStksMREEG-------GFEVIKKAILNL---SLRHKEHISAY---GEGNERRLTGKH 356
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15600312  328 EAPVMLAYS--ARNRSASIRIPYVSSPKAR-RIEARFPDPAANPYLAFAAL 375
Cdd:PLN03036 357 ETASIDTFSwgVANRGCSIRVGRDTEKKGKgYLEDRRPASNMDPYIVTSLL 407
 
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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