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Conserved domains on  [gi|2117971684|ref|XP_044277468|]
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glutamate--cysteine ligase catalytic subunit [Varanus komodoensis]

Protein Classification

glutamate--cysteine ligase( domain architecture ID 10503665)

glutamate--cysteine ligase catalyzes the rate limiting step in the biosynthesis of glutathione, the formation of L-gamma-glutamyl-L-cysteine from L-cysteine and L-glutamate

CATH:  3.30.590.20
EC:  6.3.2.2
Gene Ontology:  GO:0005524|GO:0004357|GO:0006750
PubMed:  18812186|22995213

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
237-609 0e+00

Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ligase (E.C. 6.3.2.2), also known as gamma-glutamylcysteine synthetase (GCS). This enzyme catalyzes the rate limiting step in the biosynthesis of glutathione. The eukaryotic enzyme is a dimer of a heavy chain and a light chain with all the catalytic activity exhibited by the heavy chain (this family).


:

Pssm-ID: 460796  Cd Length: 369  Bit Score: 747.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 237 VYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAAAPFYRGYVTDIDCRWGVISASVDDRTREERGLE 316
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAKNIDEARYLYDQLAPLAPIMLALTAASPIYKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 317 PLKNNhyRIHKSRYDSIDSYLSE---CGEKYNDIDLTIDKEIYEHLIKEGIDHLLAQHIAHLFIRDPLTLFEEKIHLDDA 393
Cdd:pfam03074  81 PLKNF--RIPKSRYDSIDLYLSGdsrLRPEYNDINLPIDEDIYKRLLENGVDELLAKHFAHLFIRDPLVIFSEKIEQDDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 394 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 472
Cdd:pfam03074 159 TSTDHFENIQSTNWQTMRFKPPPPNSDkIGWRVEFRPMEVQLTDFENAAYSVFIVLLTRAILSFKLNFYIPISKVDENME 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 473 VAQKRDAVRQGMFYFRKDICKGGNAVVDGCGPAQNgtetdaEEYILMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 552
Cdd:pfam03074 239 RAHKRDAVLNEKFYFRKNIFSNGSPAEDGCSSSVE------DEYELMTIDEIINGKEGGFPGLIPLIRSYLDSVNVDVDT 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2117971684 553 RCSILNYLKLIKKRASGELMTAARWMREFVANHPEYKHDSVITEEMNYSLMWKCNQI 609
Cdd:pfam03074 313 RCRLYQYLKLISKRASGELPTAARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 369
 
Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
237-609 0e+00

Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ligase (E.C. 6.3.2.2), also known as gamma-glutamylcysteine synthetase (GCS). This enzyme catalyzes the rate limiting step in the biosynthesis of glutathione. The eukaryotic enzyme is a dimer of a heavy chain and a light chain with all the catalytic activity exhibited by the heavy chain (this family).


Pssm-ID: 460796  Cd Length: 369  Bit Score: 747.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 237 VYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAAAPFYRGYVTDIDCRWGVISASVDDRTREERGLE 316
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAKNIDEARYLYDQLAPLAPIMLALTAASPIYKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 317 PLKNNhyRIHKSRYDSIDSYLSE---CGEKYNDIDLTIDKEIYEHLIKEGIDHLLAQHIAHLFIRDPLTLFEEKIHLDDA 393
Cdd:pfam03074  81 PLKNF--RIPKSRYDSIDLYLSGdsrLRPEYNDINLPIDEDIYKRLLENGVDELLAKHFAHLFIRDPLVIFSEKIEQDDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 394 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 472
Cdd:pfam03074 159 TSTDHFENIQSTNWQTMRFKPPPPNSDkIGWRVEFRPMEVQLTDFENAAYSVFIVLLTRAILSFKLNFYIPISKVDENME 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 473 VAQKRDAVRQGMFYFRKDICKGGNAVVDGCGPAQNgtetdaEEYILMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 552
Cdd:pfam03074 239 RAHKRDAVLNEKFYFRKNIFSNGSPAEDGCSSSVE------DEYELMTIDEIINGKEGGFPGLIPLIRSYLDSVNVDVDT 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2117971684 553 RCSILNYLKLIKKRASGELMTAARWMREFVANHPEYKHDSVITEEMNYSLMWKCNQI 609
Cdd:pfam03074 313 RCRLYQYLKLISKRASGELPTAARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 369
 
Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
237-609 0e+00

Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ligase (E.C. 6.3.2.2), also known as gamma-glutamylcysteine synthetase (GCS). This enzyme catalyzes the rate limiting step in the biosynthesis of glutathione. The eukaryotic enzyme is a dimer of a heavy chain and a light chain with all the catalytic activity exhibited by the heavy chain (this family).


Pssm-ID: 460796  Cd Length: 369  Bit Score: 747.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 237 VYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAAAPFYRGYVTDIDCRWGVISASVDDRTREERGLE 316
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAKNIDEARYLYDQLAPLAPIMLALTAASPIYKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 317 PLKNNhyRIHKSRYDSIDSYLSE---CGEKYNDIDLTIDKEIYEHLIKEGIDHLLAQHIAHLFIRDPLTLFEEKIHLDDA 393
Cdd:pfam03074  81 PLKNF--RIPKSRYDSIDLYLSGdsrLRPEYNDINLPIDEDIYKRLLENGVDELLAKHFAHLFIRDPLVIFSEKIEQDDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 394 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 472
Cdd:pfam03074 159 TSTDHFENIQSTNWQTMRFKPPPPNSDkIGWRVEFRPMEVQLTDFENAAYSVFIVLLTRAILSFKLNFYIPISKVDENME 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117971684 473 VAQKRDAVRQGMFYFRKDICKGGNAVVDGCGPAQNgtetdaEEYILMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 552
Cdd:pfam03074 239 RAHKRDAVLNEKFYFRKNIFSNGSPAEDGCSSSVE------DEYELMTIDEIINGKEGGFPGLIPLIRSYLDSVNVDVDT 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2117971684 553 RCSILNYLKLIKKRASGELMTAARWMREFVANHPEYKHDSVITEEMNYSLMWKCNQI 609
Cdd:pfam03074 313 RCRLYQYLKLISKRASGELPTAARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 369
 
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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