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Conserved domains on  [gi|308199423|ref|NP_001184044|]
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glutamate--cysteine ligase catalytic subunit isoform b [Homo sapiens]

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 ...
198-570 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: 754.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  198 IYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLE 277
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAKNIDEARYLYDQLAPLAPIMLALTAASPIYKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  278 PLKNNnyRISKSRYDSIDSYLSK---CGEKYNDIDLTIDKEIYEQLLQEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDA 354
Cdd:pfam03074  81 PLKNF--RIPKSRYDSIDLYLSGdsrLRPEYNDINLPIDEDIYKRLLENGVDELLAKHFAHLFIRDPLVIFSEKIEQDDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  355 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 433
Cdd:pfam03074 159 TSTDHFENIQSTNWQTMRFKPPPPNSDkIGWRVEFRPMEVQLTDFENAAYSVFIVLLTRAILSFKLNFYIPISKVDENME 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  434 VAQKRDAVLQGMFYFRKDICKGGNAVVDGCGKAQNstelaaEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 513
Cdd:pfam03074 239 RAHKRDAVLNEKFYFRKNIFSNGSPAEDGCSSSVE------DEYELMTIDEIINGKEGGFPGLIPLIRSYLDSVNVDVDT 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 308199423  514 RCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSLILKCNQI 570
Cdd:pfam03074 313 RCRLYQYLKLISKRASGELPTAARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 369
PRK00087 super family cl35061
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
22-76 5.84e-03

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


The actual alignment was detected with superfamily member PRK00087:

Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 39.54  E-value: 5.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 308199423  22 VRRHGILQFLHI----YHAVKdRHKDVLKWGDEVEYMLVSFDHENKKVRlvLSGEKVLE 76
Cdd:PRK00087 495 VDIGGVDGLLHVseisWGRVE-KPSDVLKVGDEIKVYILDIDKENKKLS--LSLKKLLP 550
 
Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
198-570 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: 754.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  198 IYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLE 277
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAKNIDEARYLYDQLAPLAPIMLALTAASPIYKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  278 PLKNNnyRISKSRYDSIDSYLSK---CGEKYNDIDLTIDKEIYEQLLQEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDA 354
Cdd:pfam03074  81 PLKNF--RIPKSRYDSIDLYLSGdsrLRPEYNDINLPIDEDIYKRLLENGVDELLAKHFAHLFIRDPLVIFSEKIEQDDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  355 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 433
Cdd:pfam03074 159 TSTDHFENIQSTNWQTMRFKPPPPNSDkIGWRVEFRPMEVQLTDFENAAYSVFIVLLTRAILSFKLNFYIPISKVDENME 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  434 VAQKRDAVLQGMFYFRKDICKGGNAVVDGCGKAQNstelaaEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 513
Cdd:pfam03074 239 RAHKRDAVLNEKFYFRKNIFSNGSPAEDGCSSSVE------DEYELMTIDEIINGKEGGFPGLIPLIRSYLDSVNVDVDT 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 308199423  514 RCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSLILKCNQI 570
Cdd:pfam03074 313 RCRLYQYLKLISKRASGELPTAARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 369
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
22-76 5.84e-03

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 39.54  E-value: 5.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 308199423  22 VRRHGILQFLHI----YHAVKdRHKDVLKWGDEVEYMLVSFDHENKKVRlvLSGEKVLE 76
Cdd:PRK00087 495 VDIGGVDGLLHVseisWGRVE-KPSDVLKVGDEIKVYILDIDKENKKLS--LSLKKLLP 550
 
Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
198-570 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: 754.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  198 IYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLE 277
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAKNIDEARYLYDQLAPLAPIMLALTAASPIYKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  278 PLKNNnyRISKSRYDSIDSYLSK---CGEKYNDIDLTIDKEIYEQLLQEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDA 354
Cdd:pfam03074  81 PLKNF--RIPKSRYDSIDLYLSGdsrLRPEYNDINLPIDEDIYKRLLENGVDELLAKHFAHLFIRDPLVIFSEKIEQDDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  355 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 433
Cdd:pfam03074 159 TSTDHFENIQSTNWQTMRFKPPPPNSDkIGWRVEFRPMEVQLTDFENAAYSVFIVLLTRAILSFKLNFYIPISKVDENME 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308199423  434 VAQKRDAVLQGMFYFRKDICKGGNAVVDGCGKAQNstelaaEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 513
Cdd:pfam03074 239 RAHKRDAVLNEKFYFRKNIFSNGSPAEDGCSSSVE------DEYELMTIDEIINGKEGGFPGLIPLIRSYLDSVNVDVDT 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 308199423  514 RCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSLILKCNQI 570
Cdd:pfam03074 313 RCRLYQYLKLISKRASGELPTAARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 369
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
22-76 5.84e-03

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 39.54  E-value: 5.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 308199423  22 VRRHGILQFLHI----YHAVKdRHKDVLKWGDEVEYMLVSFDHENKKVRlvLSGEKVLE 76
Cdd:PRK00087 495 VDIGGVDGLLHVseisWGRVE-KPSDVLKVGDEIKVYILDIDKENKKLS--LSLKKLLP 550
rpsA PRK06299
30S ribosomal protein S1; Reviewed
26-67 7.66e-03

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 38.99  E-value: 7.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 308199423  26 GILQFLHIYHAVKDRHKD---VLKWGDEVEYMLVSFDHENKKVRL 67
Cdd:PRK06299 483 GVEGLIRASELSRDRVEDateVLKVGDEVEAKVINIDRKNRRISL 527
 
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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